110-60-1

Hazards Identification

Hazards Summary:

Corrosive to rabbit skin; Causes severe damage to rabbit eyes; [ToxPlanet: EFSA: DAR - Vol. 1] Cause muscle contraction or spasticity in intraperitoneal lethal-doses studies of mice; Causes somnolence, ptosis, and urine changes in oral lethal-dose studies of rats; [RTECS] Causes burns; Inhalation may cause corrosive injuries to upper respiratory tract and lungs; Harmful by ingestion and skin absorption; Toxic by inhalation; Reproductive effects observed in experimental animals; [Alfa Aesar MSDS]

Usage

Uses

1. Used in Biological Systems:
1,4-Diaminobutane is used as a GABA precursor in many biological systems, playing a crucial role in cellular processes.
2. Used in Chemical Synthesis:
1,4-Diaminobutane is used as a synthon for amido-ureas, contributing to the development of various chemical compounds.
3. Used in Nylon Production:
1,4-Diaminobutane is involved in the synthesis of nylon 46 by reacting with adipic acid, making it an essential component in the production of this type of nylon.
4. Used in the Study of Polyamines:
1,4-Diaminobutane, along with cadaverine, spermine, and spermidine, is studied as part of the polyamines group, which are molecules containing two or more amino groups. These compounds are found in all cell types and have various functions in different cell types.
5. Used in Food Industry:
Putrescine is present in various kinds of foodstuffs, partly due to their endogenous origin. The largest amount of putrescine in humans is taken from food, and it plays a role in normal metabolism when consumed in appropriate amounts. However, increased intake of putrescine in food can lead to serious toxicological consequences.

Biosynthesis

l ,4-Diaminobutane (putrescine), spermidine, spermine, and closely related derivatives are found in a wide variety of animals, bacteria, yeasts, and plants. It is generally accepted that polyamine biosynthesis is intimately interrelated with the synthesis of nucleic acids and proteins[3]. Polyamines are ubiquitous in biological materials, although the relative amounts of 1,4-diaminobutane, spermidine, and spermine differ markedly in different cells[4, 5]. In general, prokaryotes have a higher concentration of 1,4-diaminobutane than spermidine and lack spermine. Eukaryotes usually have little 1,4-diaminobutane, and have spermine as well as spermidine. The pathway for the biosynthesis of 1,4-diaminobutane and spermidine was first established in microorganisms and was later found to be very similar in animal cells. In bacteria, 1,4-diaminobutane may be formed either by ornithine decarboxylase or by arginine decarboxylase via agmatine[6-8]. Both biosynthetic enzymes are normally present in Escherichia coli, although ornithine decarboxylation is usually the major pathway[8]. Both decarboxylases have been purified from E. coli and have been shown to require pyridoxal phosphate[9-11]. These enzymes are subject to feedback inhibition and repression by 1,4-diaminobutane or spermidine[12, 13]. In animal tissues amines are derived by decarboxylation of ornithine, rather than by decarboxylation of arginine[14, 15]. Purification of ornithine decarboxylase has been hindered by the very low enzyme activity normally present. However, as discussed in the section on the role of polyamines in growth, ornithine decarboxylase levels increase dramatically after a variety of stimuli, and the enzyme has been purified to apparent homogeneity from regenerating liver[17] and from the livers of rats treated with thioacetamide[18]. Pyridoxal phosphate appears to be a required cofactor[16, 19].

Physiological function

Putrescine fulfills important physiological functions in a wide variety of living cells. This BA shows many physiological functions and it is a precursor in the synthesis of other polyamines (spermine and spermidine). Putrescine is classified as a physiologic amine. Physiological functions of putrescine and other polyamines are related to their polycationic nature, which determines interactions with negatively charged molecules such as DNA, RNA, proteins, phospholipids[20]. Newer studies show that putrescine, along with other polyamines and phosphate ions, forms nuclear aggregates of polyamines in the cell nuclei, which are responsible for the abovementioned interactions and affect the 3-dimensional structure of DNA[21]. These interactions are related to the regulation of the structure of nucleic acids and protein synthesis[22, 23]. Putrescine, along with other polyamines, binds to membrane structures such as phospholipids, mainly in erythrocytes. This polyamine may lead to a decrease in membrane fluidity but also to increased resistance to fragmentation due to stabilization of the membrane skeleton[24, 25]. It has also been found that apart from the membrane stabilization and the effect on the synthesis of nucleic acids and proteins, polyamines are involved in the removal of free radicals[26]. In many mammals, they play an important role as luminal growth factors for intestinal maturation and growth[27, 28] and can play a significant role in the prevention of food allergies[29]. In mammals, polyamines have direct effects on several ion channels and receptors, resulting in the regulation of Ca2+, Na+, and K+ homeostasis[30, 31].

Toxicity

With respect to important physiological functions, it is clear that disruption of the normal balance due to increased intake of putrescine from food can have serious toxicological consequences. Although the toxic effects of putrescine are significantly lower than that of histamine or tyramine, there are many serious secondary effects. Diamines such as putrescine have a very important role in alimentary poisoning as they can enhance and potentiate the toxic effect of histamine, tyramine, and phenylethylamine by interacting with enzymes that metabolize these BAs[33]. For example, experiments on guinea pigs and rats revealed that putrescine potentiates histamine toxicity up to 10 times[34, 35]. Putrescine enhances histamine toxicity by inhibiting enzymes oxidizing histamine diaminooxidase(DAO; EC 1.4.3.6)?and histamine N-methyltransferase (NMT; EC 2.1.1.8)[36-38]. Moreover, from a toxicological point of view, a serious aspect of putrescine occurrence in foodstuffs is the possibility of forming carcinogenic nitrosamines. Putrescine can form carcinogenic nitrosamines by the reaction with nitrites[39, 40].

The effect of putrescine on food quality

In addition to the toxic effects, the occurrence of putrescine in foodstuffs leads to undesirable organoleptic properties and adversely affects the taste and aroma of food[41], for example, in shrimps, it is perceptible at concentrations of 3 mg/kg[42]. Increased occurrence of putrescine indicates food spoilage caused by microbial activity and it is also the main BA that indicates spoiled meat. The amount of putrescine, histamine, and cadaverine shows the freshness of meat and is defined as biogenic amines index (BAI)[43].

Reference

Smith TA. 1981. Amines in food. Food Chem 6[3]:169–200. Bard′ocz S, Duguid TJ, Brown DS, Grant G, Pusztai A, White A, Ralph A. 1995. The importance of dietary polyamines in cell regeneration and growth. Br J Nutr 73[6]:819–28. Guggenheim, M. 1 9 5 1 . Die biogenell Amine. Switzerland: Karger. 4th ed. Tabor, H., Tabor, C. W. 1964. Pharmacal. Rev. 1 6:245-300 Tabor, H., Tabor, C. W. 1972. Adv. Enzymol. 36:203-68 Morris, D. R., Fillingame, R. H. 1974. Ann. Rev. Biochem. 43:303-25 Morris, D. R., Pardee, A. B. 1966. J. Bio. Chem. 241:3 129-35 Morris, D. R., Koffron, K. L. 1969. J. Bio. Chem. 244:6094-99 Applebaum, D. 1972. Purification and characterization of induced and biosynthetic ornithine decarboxylases of Escherichia coli. PhD thesis. Univ. Washington. Seattle. 157 pp. Univ. Microfilms #73-1 3789 Wu, W. H., Morris, D. R. 1973. J. Bio. Chem. 248: 1687-95, 1696-99 Holtta, E., Janne, J., Pispa, J. 1972. Biochem. Biophys. Res. Commun. 47: 1165-71 Tabor, H., Tabor. C. W. 1969. J. Bio. Chem. 244:2286-92 Morris, D. R., Wu, W. H., Applebaum, D., Kofi'ron, K. L. 1970. See Ref. 8, pp. 968-76 Russell, D. H., cd. 1973. Polyamines in Normal and Neoplastic Growth, New York: Raven. 429 pp. Herbst, E. J., Bachrach, U.,cds. 1970. Ann. NY Acad. Sci. 171:693-1009 Pegg. A. E . . Williams-Ashman. H. G. 1968. Biochem. J 108: 533-39 Friedman, S. J., Halpern, K. Y., Canellakis, E. S. 1972. Biochim. Biophys. Acta 261:181-87 Ono, M., Inoue, H., Suzuki, F., Takeda, Y. 1972. Biochim. Biophys. Acta 284:285-97 Raina, A., Jiinne, J. 1968. Acta Chem. Scand. 22 :2375-77 Igarashi K, Kashiwagi K. 2010. Modulation of cellular function by polyamines. Intl J Biochem Cell Biol 42[1]:39–51. Di Luccia A, Picariello G, Iacomino G, Formisano A, Paduano L, D’Agostino L. 2009. The in vitro nuclear aggregates of polyamines. FEBS J 276[8]:2324–35. Silla Santos MH. 1996. Biogenic amines: their importance in foods. Intl J Food Microbiol 29[2–3]:213–31. Hou MH, Lin SB, Yuann JM, Lin WC, Wang AH, Kan Ls L. 2001. Effects of polyamines on the thermal stability and formation kinetics of DNA duplexes with abnormal structure. Nucleic Acids Res 29[24]:5121–8. Til HP, Falke HE, Prinsen MK, Willems MI. 1997. Acute and subacute toxicity of tyramine, spermidine, spermine, putrescine and cadaverine in rats. Food Chem Toxicol 35[3–4]:337–48. Largue E, Sabater-Molina M, Zamora S. 2007. Biological significance of dietary polyamines. Nutrition 23[1]:87–95. Kaur-Sawhney R, Tiburcio AF, Altabella T, Galston AW. 2003. Polyamines in plants: an overview. J Cell Mol Biol 2:1–12. Dufour C, Dandrifosse G, Forget P, Vermesse F, Romain N, Lepoint P. 1988. Spermine and spermidine induce intestinal maturation in the rat. Gastroenterology 95[1]:112–6. L¨oser C. 2000. Polyamines in human and animal milk. Br J Nutr 84[Suppl1]:S55–8 Dandrifosse G, Peulen O, El Khefif N, Deloyer P, Dandrifosse AC, Grandfils C. 2000. Are milk polyamines preventive agents against food allergy? Proc Nutr Soc 59[1]:81–6. Dandrifosse G, Peulen O, El Khefif N, Deloyer P, Dandrifosse AC, Grandfils C. 2000. Are milk polyamines preventive agents against food allergy? Proc Nutr Soc 59[1]:81–6. Johnson TD. 1996. Modulation of channel function by polyamines. Trends Pharmacol Sci 17[1]:22–7. Li J, Doyle KM, Tatlisumak T. 2007. Polyamines in the brain: distribution, biological interactions, and their potential therapeutic role in brain ischemia. Curr Med Chem 14[17]:1807– https://www.alfa.com/zh-cn/catalog/B21316/ Taylor SL. 1985a. Histamine food poisoning: toxicology and clinical aspects. Crit Rev Toxicol 17[2]:91–128. Parrot J, Nicot G. 1966. Pharmacology of histamine. In: Eichler O, Farah S, editors. Handbook of experimental pharmacology. Heidelberg: Springer-Verlag. p 148–61. Lehane L, Olley J. 2000. Histamine fish poisoning revisited. Intl J Food Microbiol 58[1–2]:1–37. Stratton JE, Hutkins RW, Taylor SL. 1991. Biogenic amines in cheese and other fermented foods: a review. J Food Prot 54[6]:460–70. Hern′andez-Jover T, Izquierdo-Pulido M, Veciana-Nogues MT, Marine-Font A, Vidal-Carou MC. 1997. Biogenic amine and polyamine contents in meat and meat products. J Agric Food Chem 45[6]:2098–102. Emborg J, Dalgaard P. 2006. Formation of histamine and biogenic amines in cold-smoked tuna: an investigation of psychrotolerant bacteria from samples implicated in cases of histamine fish poisoning. J Food Prot 69[4]:897–906. Shalaby AR. 1996. Significance of biogenic amines to food safety and human health. Food Res Intl 29[7]:675–90. Bover-Cid S, Holzapfel WH. 1999. Improved screening procedure for biogenic amine production by lactic acid bacteria. Intl J Food Microbiol 53[1]:33–41. Lehane L, Olley J. 2000. Histamine fish poisoning revisited. Intl J Food Microbiol 58[1–2]:1–37. Benner Jr RA, Staruszkiewicz WF, Rogers PL, Otwelle WS. 2003. Evaluation of putrescine, cadaverine, and indole as chemical indicators of decomposition in penaeid shrimp. J Food Sci 68[7]:2178–85. Karmas E. 1981. Biogenic amines as indicators of sea food freshness. Lebensmitt Wissensch Technol Food Sci Technol 14[5]:273–5.

Safety Profile

Poison by subcutaneous, intravenous, and rectal routes. Moderately toxic by ingestion. An experimental teratogen. Human mutation data reported. When heated to decomposition it emits toxic fumes of NOx. See also 1,3-BUTANEDIAMINE and AMINES.

InChI:InChI=1/C4H12N2/c5-3-1-2-4-6/h1-6H2

Synthetic route

putrescine dihydrochloride (333-93-7) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With potassium hydroxide In tetrahydrofuran at 20℃; for 12h; Inert atmosphere;	95.4%

butanedinitrile (110-61-2) → 2-pyrrolidinon (616-45-5) + acrylobutyronitril + 1,4-diaminobutane (110-60-1)

Conditions	Yield
With rubidium hydroxide; hydrogen; ethylenediamine; RaNi catalyst doped with Fe and Cr, slurry in water In water at 80℃; under 525053 Torr; Product distribution / selectivity;	A 3% B 1% C 92%
With cesium hydroxide; hydrogen; ethylenediamine; RaNi catalyst doped with Fe and Cr, slurry in water In water at 80℃; under 525053 Torr; Product distribution / selectivity;	A 3% B 5% C 90%
With sodium hydroxide; hydrogen; ethylenediamine; RaNi catalyst doped with Fe and Cr, slurry in water In water at 80℃; under 525053 Torr; Product distribution / selectivity;	A 4% B 5% C 85%

succinaldehyde dioxime (2580-71-4) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With ammonium formate; zinc In methanol for 0.133333h; Heating;	91%
With ammonium formate; magnesium In methanol at 20℃; for 0.833333h;	81%
With hydrogenchloride; ethanol; water Hydrogenation.an Platin;
With ethanol; sodium bei Siedehitze;
With sodium amalgam; ethanol; acetic acid at 50 - 60℃;

4-aminobutyronitrile (32754-99-7) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With sodium tetrahydroborate; nickel dichloride In ethanol; acetonitrile at 20℃;	79%

1,2-diazine (289-80-5) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With Cp*Rh(2-(2-pyridyl)phenyl)H; hydrogen In neat (no solvent) at 100℃; under 27361.8 Torr; for 48h; Catalytic behavior; Glovebox;	78%
With potassium hydroxide; aluminum nickel for 2.5h;	61%
With ethanol; sodium

butanedinitrile (110-61-2) → pyrrolidine (123-75-1) + 1,4-diaminobutane (110-60-1)

Conditions	Yield
With ammonia; nickel at 140℃; under 80905.8 Torr; Hydrogenation;

butanedinitrile (110-61-2) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With cobalt catalyst; ammonia at 120℃; under 62518.2 - 154457 Torr; Hydrogenation;
With Methyl formate; cobalt catalyst at 65 - 85℃; under 102971 - 154457 Torr; Hydrogenation.anschl. Eindampfen mit konz. HCl;
With ethanol; ammonia; nickel at 100℃; under 62518.2 Torr; Hydrogenation;

phthalimide (136918-14-4) + 1,4-dichlorobutane (110-56-5) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With potassium carbonate; N,N-dimethyl-formamide anschl. mit wss. NaOH;

Adipic acid (124-04-9) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With chloroform; tris-(2-chloro-ethyl)-amine; sulfuric acid at 40℃;
With chloroform; tris-(2-chloro-ethyl)-amine; sulfuric acid at 40℃;
With chloroform; tris-(2-chloro-ethyl)-amine; sulfuric acid at 40℃;

2,5-diaminopentanoic acid (70-26-8, 348-66-3, 616-07-9, 7006-33-9) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
durch Einwirkung von Clostridium septicum;
durch Einwirkung von Proteus vulgaris;
durch Einwirkung von Proteus morganii;
durch Einwirkung von Escherichia coli;

L-ornithine (70-26-8) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
bei der Einw. von Faeulnisbakterien;
unter der Einwirkung von Ornithin-Decarboxylase-Praeparaten aus Escherichia coli, Proteus vulgaris, Proteus morganii und Clostridium septicum;
With sodium acetate buffer; lysine decarboy;ase from Selenomonas ruminantium In water at 40℃; for 0.333333h; pH=6.0; Enzyme kinetics; Decarboxylation;
With ornithine decarboxylase from Saccharomyces cerevisiae; pyridoxal 5'-phosphate; potassium chloride; triethylamine at 25℃; Kinetics; Enzymatic reaction;

L-arginine (74-79-3) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
durch Salmonella enteritidis;

L-arginine (74-79-3) → 1,4-diaminobutane (110-60-1) + 5-aminopentanoic acid (660-88-8)

Conditions	Yield
bei der Einw. von Faeulnisbakterien;

adipamide (628-94-4) → 1,4-diaminobutane (110-60-1)

arcaine (544-05-8) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
durch Einwirkung von Faeulnisbakterien;

uvariadiamide (31991-78-3) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With hydrogenchloride

N-(4-aminobutyl)benzamide (5692-23-9) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With hydrogenchloride

1,4-bis(phthalimido)butane (3623-90-3) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With hydrogenchloride at 130℃;
With hydrogenchloride at 230℃;

Adipic acid dichloride (111-50-2) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With sodium azide; benzene anschl. Erhitzen mit HCl;

adipic acid dihydrazide (1071-93-8) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With hydrogenchloride; sodium nitrite anschl. Erwaermen der aether. Loesung und Behandeln mit heisser konz. HCl;

(1E,3E)-1,4-dichloro-1,4-dinitro-buta-1,3-diene (13105-37-8) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With hydrogen; platinum on activated charcoal In ethanol

2-ethylaziridine (2549-67-9) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With ammonia

Spermine (71-44-3) → N-(3-aminopropyl)-1,4-diaminobutane (124-20-9) + 1,4-diaminobutane (110-60-1) + acrolein (107-02-8)

Conditions	Yield
With phosphate buffer In water at 37℃; Product distribution; bovine serum amine oxidase; other polyamines;

kinetin (525-79-1) → N-(3-aminopropyl)-1,4-diaminobutane (124-20-9) + Spermine (71-44-3) + 1,4-diaminobutane (110-60-1)

Conditions	Yield
at 30℃; for 24h; effect on poliamine content and ratio in rice embryos of Oryza sativa;

(R)-(-)-abscisic acid (14398-53-9) → N-(3-aminopropyl)-1,4-diaminobutane (124-20-9) + Spermine (71-44-3) + 1,4-diaminobutane (110-60-1)

Conditions	Yield
at 30℃; for 24h; effect on poliamine content and ratio in rice embryos of Oryza sativa;

1-buten-3 (88211-46-5) → 1,4-diaminobutane (110-60-1)

Conditions	Yield
With sodium hypochlorite; dimethylborane; ammonia 1.) 0 deg C, 1 h, 2.) O deg C; Yield given. Multistep reaction;

N1-(10-Methyl-9,10-dihydro-acridin-9-yl)-butane-1,4-diamine → N-methylacridinium iodide (948-43-6) + 1,4-diaminobutane (110-60-1)

Conditions	Yield
With butane-1,4-diamine; monoprotonated form In acetonitrile at 25℃; Equilibrium constant;

4-(4-Amino-butylamino)-1-benzyl-1,4-dihydro-quinoline-3-carbonitrile → 1-benzyl-3-cyanoquinolinium tetrafluoroborate + 1,4-diaminobutane (110-60-1)

Conditions	Yield
With butane-1,4-diamine; monoprotonated form In acetonitrile at 25℃; Equilibrium constant;

N-(3-aminopropyl)-1,4-diaminobutane (124-20-9) → 3-aminopropanal (352-92-1) + 1,4-diaminobutane (110-60-1)

Conditions	Yield
With phosphate buffer (pH: 5.5); oxygen at 35℃; for 0.333333h; Product distribution; polyamine oxidase of Penicillium chrysogenum; further enzyme;

Spermine (71-44-3) → 3-aminopropanal (352-92-1) + 1,4-diaminobutane (110-60-1)

Conditions	Yield
With phosphate buffer (pH: 5.5); oxygen at 35℃; for 0.333333h; Product distribution; polyamine oxidase of Penicillium chrysogenum; further enzyme;

1,4-diaminobutane (110-60-1) + acrylonitrile (107-13-1) → 3-(4-[(2-cyanoethyl)amino]butylamino)propanenitrile (14209-32-6)

Conditions	Yield
In methanol at 0 - 20℃; for 18h;	100%
In methanol at 0 - 20℃; for 18h;	100%
for 2h; 0 deg C->r. t.;	97%

benzaldehyde (100-52-7) + 1,4-diaminobutane (110-60-1) → N,N-bis-(phenylmethylene)butane-1,4-diamine (6970-47-4)

Conditions	Yield
In ethanol Heating;	100%
With magnesium sulfate In methanol for 1h; Ambient temperature;

di-tert-butyl dicarbonate (24424-99-5) + 1,4-diaminobutane (110-60-1) → 1-amino-4-[(tert-butyloxycarbonyl)amino]butane (68076-36-8)

Conditions	Yield
In chloroform 1.) 3 h, ice bath, 2.) room temperature, 16 h;	100%
In chloroform for 18h;	100%
In chloroform at 20℃;	100%

di-tert-butyl dicarbonate (24424-99-5) + 1,4-diaminobutane (110-60-1) → 1-amino-4-[(tert-butyloxycarbonyl)amino]butane (68076-36-8) + 1,4-bis(tert-butoxycarbonylamino)butane (33545-97-0)

Conditions	Yield
In chloroform at 0 - 20℃; for 16.5h;	A 100% B n/a
In 1,4-dioxane at 20℃; Inert atmosphere;	A 95% B 5%
In 1,4-dioxane for 22h;	A 85% B 5%
In methanol at 0℃; for 0.0166667h; Flow reactor;	A 65% B n/a

2-(vinyloxy)ethyl isothiocyanate (59565-09-2) + 1,4-diaminobutane (110-60-1) → 1-(2-Vinyloxy-ethyl)-3-{4-[3-(2-vinyloxy-ethyl)-thioureido]-butyl}-thiourea (140455-24-9)

Conditions	Yield
for 0.0833333h;	100%

C106H123N37O59P9(9-) + 1,4-diaminobutane (110-60-1) → C101H123N39O58P9(9-)

Conditions	Yield
In water at 65℃; for 14h;	100%

di-tert-butyl dicarbonate (24424-99-5) + 1,4-diaminobutane (110-60-1) → 1,4-bis(tert-butoxycarbonylamino)butane (33545-97-0)

Conditions	Yield
aminosulfonic acid at 25 - 28℃; for 0.05h;	100%
In neat (no solvent) at 80℃; for 0.166667h; Green chemistry; chemoselective reaction;	97%
With triethylamine In dichloromethane at 20℃; for 12h; Product distribution / selectivity;	94.5%

1,4-diaminobutane (110-60-1) + cis-2-<<(tert-butyldiphenylsilyl)oxy>methyl>-5-4-(p-tolylsulfonyl)cytosin-1'-yl>-1,3-oxathiolane → cis-2-<(tert-butyldiphenyl)silyloxymethyl>-5-4-(4-aminobutyl)cytosin-1'-yl>-1,3-oxathiolane

Conditions	Yield
With lutidine at 90℃; for 48h;	100%

4,7-dichloroquinoline (86-98-6) + 1,4-diaminobutane (110-60-1) → N1-(7-chloroquinolin-4-yl)butane-1,4-diamine (53186-45-1)

Conditions	Yield
Inert atmosphere;	100%
at 95℃; for 1h; Microwave irradiation;	100%
In isopropyl alcohol at 100℃; for 20h;	99%

1,4-diaminobutane (110-60-1) + ethyl (+)-(3R,7Z)-3-{[(4-methylphenyl)sulfonyl]amino}dec-7-enoate (467457-05-2) → (3R,7Z)-N-(4-aminobutyl)-3-{[(4-methylphenyl)sulfonyl]amino}dec-7-enamide (467457-07-4)

Conditions	Yield
copper diacetate at 20℃; for 8h;	100%

1,4-diaminobutane (110-60-1) + ethyl (+)-(3S)-3-{[(4-methylphenyl)sulfonyl]amino}-4-(octylthio)butanoate (467457-49-4) → (+)-(3S)-N-(4-aminobutyl)-3-{[(4-methylphenyl)sulfonyl]amino}-4-(octylthio)butanamide (467457-51-8)

Conditions	Yield
With copper diacetate at 20℃; for 8h;	100%

1,4-diaminobutane (110-60-1) + 8-bromo-2',3'-O-isopropylene adenosine (13089-45-7) → 8-amino[1''-(4''-aminobutyl)]-2',3'-O-isopropylidene adenosine (256953-64-7)

Conditions	Yield
With triethylamine In dimethyl sulfoxide at 110℃; for 4h;	100%
With triethylamine In dimethyl sulfoxide at 110℃; for 4h;	99%

1,4-diaminobutane (110-60-1) + 3β-(4'-chlorophenyl)tropane-2β-carboxylic acid → 1,4-di-(3β-(p-chlorophenyl)tropane-2β-carboxamide)-butane

Conditions	Yield
Stage #1: 3β-(4'-chlorophenyl)tropane-2β-carboxylic acid With (benzotriazo-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate; triethylamine In dichloromethane at 0℃; for 0.5h; Stage #2: 1,4-diaminobutane In dichloromethane at 20℃;	100%

1,4-diaminobutane (110-60-1) + N-carboxyethylchitin ethyl ester; Mn=12000, Mw=49000, degree of CO2Et substitution per sugar unit =1.17 → N-carboxyethylchitin 4-aminobutylamide

Conditions	Yield
In ethanol; water at 70℃; for 24h;	100%

{4-[tert-butoxycarbonyl-(2-oxo-tetrahydro-furan-3-ylmethyl)-amino]-butyl}-carbamic acid tert-butyl ester (860495-53-0) + 1,4-diaminobutane (110-60-1) → [2-(4-amino-butylcarbamoyl)-4-hydroxy-butyl]-(4-tert-butoxycarbonylamino-butyl)-carbamic acid tert-butyl ester (860495-54-1)

Conditions	Yield
In ethanol at 20℃; for 18h;	100%

1,4-diaminobutane (110-60-1) + 2-Bromoacetyl bromide (598-21-0) → N,N′-(butane-1,4-diyl) bis(2-bromoethanamide)

Conditions	Yield
With potassium carbonate In dichloromethane; water at 5 - 20℃; for 12h;	100%
With potassium carbonate In chloroform; water at 5 - 20℃; for 24.5h;	99%
With sodium hydroxide In diethyl ether; water for 1h; pH=10 - 11; cooling;	85%
With potassium carbonate In dichloromethane; water at 0 - 20℃; for 24h;	57%

3-pyridinecarboxaldehyde (500-22-1) + 1,4-diaminobutane (110-60-1) → N,N-bis-(pyridin-3-ylmethylene)butane-1,4-diamine

Conditions	Yield
In ethanol Heating;	100%

formaldehyd (50-00-0) + 4-nitro-aniline (100-01-6) + 1,4-diaminobutane (110-60-1) → 1-(p-nitrophenyl)-2-[3-{3-[2-(p-nitrophenyl)-1-diazenyl]-1,3-diazepan-1-ylmethyl}-1,3-diazepan-1-yl]diazene

Conditions	Yield
Stage #1: 4-nitro-aniline With hydrogenchloride; sodium nitrite at 0 - 5℃; for 0.5h; Stage #2: formaldehyd; 1,4-diaminobutane With sodium hydrogencarbonate In water for 0.5h; cooling;	100%

formaldehyd (50-00-0) + 4-aminobenzamide (2835-68-9) + 1,4-diaminobutane (110-60-1) → 4-(2-{3-[(3-{2-[4-(aminocarbonyl)phenyl]-1-diazenyl}-1,3-diazepan-1-yl)methyl]-1,3-diazepan-1-yl}-1-diazenyl)benzamide

Conditions	Yield
Stage #1: 4-aminobenzamide With hydrogenchloride; sodium nitrite at 0 - 5℃; for 0.5h; Stage #2: formaldehyd; 1,4-diaminobutane With sodium hydrogencarbonate In water for 0.5h; cooling;	100%

formaldehyd (50-00-0) + 1,4-diaminobutane (110-60-1) + 4-Aminobenzonitrile (873-74-5) → 1-(p-cyanophenyl)-2-[3-{3-[2-(p-cyanophenyl)-1-diazenyl]-1,3-diazepan-1-ylnmethyl}-1,3-diazepan-1-yl]-1-diazene

Conditions	Yield
Stage #1: 4-Aminobenzonitrile With hydrogenchloride; sodium nitrite at 0 - 5℃; for 0.5h; Stage #2: formaldehyd; 1,4-diaminobutane With sodium hydrogencarbonate In water for 0.5h; cooling;	100%

1,4-diaminobutane (110-60-1) + 9-anthracene aldehyde (642-31-9) → 1,2-bis[(anthracen-9-ylmethylene)amino]butane-1,4-diamine

Conditions	Yield
With acetic acid In ethanol Heating;	100%
In methanol; dichloromethane for 4h; Heating;
In methanol; dichloromethane for 4h; Reflux;

(Z)-2-ethoxycarbonyl-2-methyl-5-(p-nitrophenoxycarbonyloxy)-[1,3]dioxane + 1,4-diaminobutane (110-60-1) → bis-1,4-{[(Z)-2-ethoxycarbonyl-2-methyl-[1,3]dioxane]-5-yloxycarbamoyl}-butane

Conditions	Yield
With triethylamine In dichloromethane at 20℃; for 2h;	100%

3-chloro-1,2,4-benzotriazine 1-oxide (67692-91-5) + 1,4-diaminobutane (110-60-1) → [4-(1-Oxido-1,2,4-benzotriazine-3-yl)butyl]-1,4-butanediamine (1073136-43-2)

Conditions	Yield
With triethylamine In dichloromethane at 20℃; for 14.5h;	100%

formaldehyd (50-00-0) + 1,4-diaminobutane (110-60-1) + diphenylphosphane (829-85-6) → (Ph2PCH2)2N(CH2)4N(CH2PPh2)2 (1119496-80-8)

Conditions	Yield
Stage #1: formaldehyd; diphenylphosphane In methanol at 70℃; for 0.5h; Inert atmosphere; Stage #2: 1,4-diaminobutane In methanol at 20℃; for 1h; Inert atmosphere; Stage #3: In methanol; toluene at 20 - 105℃; for 15h; Inert atmosphere;	100%

3-methoxy-2-hydroxybenzaldehyde (148-53-8) + 1,4-diaminobutane (110-60-1) → bis(2-hydroxy-3-methoxy-benzylidene)-tetramethylene-diamine (104978-24-7)

Conditions	Yield
In methanol for 3h; Reflux;	100%
In ethanol Reflux;

1,4-diaminobutane (110-60-1) + isovaleraldehyde (590-86-3) → N,N-diisopentylbutane-1,4-diamine (1432473-26-1)

Conditions	Yield
With sodium tetrahydroborate In ethanol for 24h;	100%

2,2,6-trimethyl-4H-1,3-dioxin-4-one (5394-63-8) + 1,4-diaminobutane (110-60-1) → (Z)-4-methyl-6,7,8,9-tetrahydro-1H-1,5-diazonin-2(5H)-one

Conditions	Yield
at 130℃; for 0.0833333h; Microwave irradiation; Green chemistry;	100%

2,3,4-tris(benzyloxy)benzoic acid (180206-32-0) + 1,4-diaminobutane (110-60-1) → C60H56N2O8

Conditions	Yield
Stage #1: 2,3,4-tris(benzyloxy)benzoic acid With benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate In dichloromethane for 0.0833333h; Stage #2: 1,4-diaminobutane With triethylamine In dichloromethane at 20℃;	100%

1,4-dinitro-1,4-diazabutane (505-71-5) + 1,4-diaminobutane (110-60-1) → 1,4-diaminium N,N'-dinitroethylenediazanide

Conditions	Yield
In water at 20℃;	100%

1,4-diaminobutane (110-60-1) + acrylonitrile (107-13-1) → 3,3′,3″,3′″-(butane-1,4-diylbis(azanetriyl))tetrapropanenitrile

Conditions	Yield
In water at 80℃; for 1h;	99%
In water at 80℃; for 1h;	99%
In water at 20 - 40℃; Temperature;	95.2%

Upstream product

• 289-80-5 1,2-diazine 
• 110-61-2 butanedinitrile 
• 136918-14-4 phthalimide 
• 110-56-5 1,4-dichlorobutane 
• 124-04-9 Adipic acid 
• 2580-71-4 succinaldehyde dioxime 
• 70-26-8 2,5-diaminopentanoic acid 
• 70-26-8 L-ornithine 
• 74-79-3 L-arginine 
• 628-94-4 adipamide 
• 544-05-8 arcaine 
• 31991-78-3 uvariadiamide 
• 5692-23-9 N-(4-aminobutyl)benzamide 
• 3623-90-3 1,4-bis(phthalimido)butane 

Downstream Products

• 78553-70-5 N,N'-tetramethylenebis(3-oxobutanamide) 
• 140926-78-9 N¹,N²-bis(7-chloroquinolin-4-yl)butane-1,4-diamine 
• 50327-22-5 1,4-bis-{5-[3-(3-methyl-5-oxo-2,5-dihydro-pyrazol-1-yl)-phenylcarbamoyl]-valerylamino}-butane 
• 129764-53-0 2,2'-diphenyl-2,2'-butanediyldiamino-di-acetonitrile 
• 31991-78-3 uvariadiamide 
• 64544-76-9 3,3'-bis-phenyl(butylene-1,4)-bisurea 
• 52420-79-8 N,N'-bis(phenylaminothiocarbonyl)-1,4-diaminobutane 
• 34062-77-6 N,N¹-(butane-1,4-diyl)bis(4-nitrobenzamide) 
• 102810-33-3 N,N'-bis-(4-methoxycarbonylbenzoyl)-1,4-butanediamine 
• 76894-37-6 2-phenyl-4,5,6,7-tetrahydro-1H-1,3-diazepine 
• 51250-16-9 S-aminobutyl-N-dithiocarbamic acid 
• 4430-51-7 1,4-butanediisothiocyanate 
• 58708-57-9 Disodium (1,4-butanediyl)bis(dithiocarbamate) 
• 4538-37-8 1,4-diisocyanatobutane 

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Amide-functionalized graphene with 1,4-DIAMINOBUTANE (cas 110-60-1) as efficient metal-free and porous electrocatalyst for oxygen reduction08/24/2019

A porous graphene catalyst was prepared with 1,4-diaminobutane (DAB) through amide functionalization and was used as a metal-free electrocatalyst for oxygen reduction reaction (ORR) in alkaline fuel cells. DAB was used as a junction among functionalized graphene layers to impart electrocatalytic...detailed

Kinetics of thermolysis of some transition metal perchlorate complexes with 1,4-DIAMINOBUTANE (cas 110-60-1) ligand☆08/23/2019

Three metal perchlorate complexes of general formula [M(dab)2](ClO4)2·xH2O (where M = Zn, Cu and Ni; dab = 1,4-diaminobutane) have been prepared and characterized by gravimetry, infrared spectroscopy (IR) and elemental analysis. Thermolysis has been studied by thermogravimetry (TG) in air and s...detailed

Molar heat capacity of aqueous solutions of 1,3-diaminopropane and 1,4-DIAMINOBUTANE (cas 110-60-1) and their piperazine blends08/22/2019

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Relevant academic research and scientific papers

Occurrence of agmatine pathway for putrescine synthesis in Selenomonas ruminatium

Selenomonas ruminantium synthesizes cadaverine and putrescine from L-lysine and L-ornithine as the essential constituents of its peptidoglycan by a constitutive lysine/ornithine decarboxylase (LDC/ODC). S. ruminantium grew normally in the presence of the specific inhibitor for LDC/ODC, DL-α-difluoromethylornithine, when arginine was supplied in the medium. In this study, we discovered the presence of arginine decarboxylase (ADC), the key enzyme in agmatine pathway for putrescine synthesis, in S. ruminantium. We purified and characterized ADC and cloned its gene (adc) from S. ruminantium chromosomal DNA. ADC showed more than 60% identity with those of LDC/ODC/ADCs from Gram-positive bacteria, but no similarity to that from Gram-negative bacteria. In this study, we also cloned the aguA and aguB genes, encoding agmatine deiminase (AguA) and N-carbamoyl-putrescine amidohydrolase (AguB), both of which are involved in conversion from agmatine into putrescine. AguA and AguB were expressed in S. ruminantium. Hence, we concluded that S. ruminantium has both ornithine and agmatine pathways for the synthesis of putrescine.

Novel characteristics of Selenomonas ruminantium lysine decarboxylase capable of decarboxylating both L-lysine and L-ornithine

Lysine decarboxylase (LDC; EC 4.1.1.18) of Selenomonas ruminantium is a constitutive enzyme and is involved in the synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth. We purified the 5. ruminantium LDC by an improved method including hydrophobic chromatography and studied the fine characteristics of the enzyme. Kinetic study of LDC showed that 5. ruminanitum LDC decarboxylated both L-lysine and L-ornithine with similar Km, and the decarboxylase activities towards both substrates were competitively and irreversibly inhibited by DL-α-difluoromethylornithine, which is a specific inhibitor of ornithine decarboxylase (EC 4.1.1.17). We also showed a drastic descent of LDC activity owing to the degradation of LDC at entry into the stationary phase of cell growth.

Turtschamide, a cytotoxic putrescine bisamide from Corydalis turtschaninovii

A putrescine bisamide with a unique cyclic structure derived from l-tyrosine, turtschamide (1), was isolated from the tubers of Corydalis turtschaninovii. The structure of 1 was established by extensive spectroscopic study, and its absolute configuration was determined by a combination of NOE experiment and application of the Marfey's method. Turtschamide (1) exhibited cytotoxicity against the A549, SK-OV-3, SK-MEL-2, and HCT-15 cells.

Analysis of catalytic determinants of diaminopimelate and ornithine decarboxylases using alternate substrates

Diaminopimelate decarboxylase (DAPDC) and ornithine decarboxylase (ODC) are pyridoxal 5′-phosphate dependent enzymes that are critical to microbial growth and pathogenicity. The latter is the target of drugs that cure African sleeping sickness, while the former is an attractive target for antibacterials. These two enzymes share the (β/α)8 (i.e., TIM barrel) fold with alanine racemase, another pyridoxal 5′-phosphate dependent enzyme critical to bacterial survival. The active site structural homology between DAPDC and ODC is striking even though DAPDC catalyzes the decarboxylation of a D stereocenter with inversion of configuration and ODC catalyzes the decarboxylation of an L stereocenter with retention of configuration. Here, the structural and mechanistic bases of these interesting properties are explored using reactions of alternate substrates with both enzymes. It is concluded that simple binding determinants do not control the observed stereochemical specificities for decarboxylation, and a concerted decarboxylation/proton transfer at Cα of the D stereocenter of diaminopimelate is a possible mechanism for the observed specificity with DAPDC.

Nickel and nickel-magnesia catalysts active in the hydrogenation of 1,4-butanedinitrile

Several NiO-MgO systems were synthesized to be studied as nickel catalysts for the hydrogenation of 1,4-butanedinitrile in the gas phase and compared with a bulk NiO of controlled morphology. All samples were characterized by XRD, BET, TPR, TPD, SEM, and H2 chemisorption techniques. The Ni-MgO systems had higher activities than the Ni bulk catalyst. The most active catalyst at all reaction temperatures was type R4CB which had homogeneous particles of about 1000 A, the highest metal surface area, and the highest coverage with weakly bound hydrogen. The presence of basic magnesia suppresses the condensation reactions and consequently favors the elimination of amines, and prevents catalyst deactivation. The selectivity toward the different products not only depends on the catalytic properties but can also be modified by controlling the hydrogen/dinitrile ratio. The highest selectivity to 4-aminobutanenitrile was achieved by catalyst R4CB, with 85% at 100% conversion and working at a space velocity of 13,000 h-1 and 343 K. This selectivity could be increased by lowering the hydrogen/butanedinitrile ratio.

Preparation and Thermal Square Planar-Octahedral Transformation of Nickel(II) Complexes Containing 1,2-Butanediamine or 3,3-Dimethyl-1,2-butanediamine in Solid Phase

Nickel(II) complexes of 1,2-butanediamine (1,2-bn) and 3,3-dimethyl-1,2-butanediamine (dmbn), were prepared, and their thermal behavior was investigated in solid phase.The original complexes were all violet, octahedral diaquabis(diamine) complexes (X2; X=Cl, Br, NO3 or ClO4).The 1,2-bn complexes with Cl- or Br- and the dmbn complex with NO3- showed a two-step thermochromism, violet->yellow->violet blue, upon heating.These steps correspond to structural changes to a square planar anhydride, and then to an octahedral dianiono complex.The complexes of both ligands with ClO4- underwent only thermal deaquation, changing into orange square planar anhydride.Other salts, the 1,2-bn complex with NO3- and the dmbn complexes with Cl- or Br-, were converted into octahedral dianiono complexes by thermal deaquation-anation which occurs in one step.The differences among the thermal reactivities of the complexes with different diamines can be understood on the basis of steric hindrance caused by the substituent groups on the diamine.

CHENGES IN POLYAMINES AND RELATED ENZYMES WITH LOSS OF VIABILITY IN RICE SEEDS.

Putrescine, spermidine and spermine of high vigour, low vigour and non viable (classes 1, 2 and 3 respectively) seeds of Oryza sativa increased with loss of viability.The largest concentration of spermine was found in non-viable embryos.Spermine was absent in the husks of all the three categories of seeds.Arginine decarboxylase was greatest in high vigoured seeds and its activity gradually declined with loss of viability.However, diamine oxidase and polyamine oxidase activities gradually increased with the loss of viability of the seeds while DNA, RNA and protein contents decreased.The total content of polyamines increased on kinetin treatment but declined on ABA treatment.DNA, RNA and protein followed the same trend as polyamines.The polyamine contents increased by ca 3- and 4-fold, respectively, in high vigoured and low vigoured seeds on 1E-4 M kinetin treatment.The activity of ADC followed the same change as that of the polyamines in both cases, but the reverse was observed for the activities of diamine and polyamine oxidases.Key Word Index - Oryza sativa; Gramineae; rice; spermine; spermidine; putrescine; arginine; arginine decarboxylase; polyamine oxidase.

Further insight into the inhibitory action of a LIM/double zinc-finger motif of an agmatinase-like protein

Agmatine is a precursor for polyamine biosynthesis also associated to neurotransmitter, anticonvulsant, antineurotoxic and antidepressant actions in the brain. It results from decarboxylation of l-arginine by arginine decarboxylase and it is hydrolyzed to urea and putrescine by agmatinase. Recently, we have described a new protein which also hydrolyzes agmatine although its sequence greatly differs from all known agmatinases. This agmatinase-like protein (ALP) contains a LIM-like double Zn-finger domain close to its carboxyl terminus, whose removal results in a truncated variant with a 10-fold increased kcat, and a 3-fold decreased Km value for agmatine. Our proposal was that the LIM-domain functions as an autoinhibitory, regulatory entity for ALP. Results in this report provide additional support for the postulated inhibitory effect. The purified isolated LIM domain was shown to be competitively inhibitory to a truncated variant ALP (lacking the LIM-domain), but not to the wild-type species. The C453A variant was shown to be a Zn2 +-free enzyme with kinetic parameters similar to those of the truncated-ALP. A molecular dynamic simulation of a modeled LIM-domain 3D structure showed that, as a consequence of C453A mutation, the coordination of the zinc ion is broken and the structure of the zinc finger is melted. The inhibitory action of the LIM/double Zinc-finger motif was associated to a significant conformational change, as detected by tryptophan fluorescence studies, but was not related to changes in the association of the enzyme with the catalytically essential Mn2 +.

Polyamine modification by acrolein exclusively produces 1,5-diazacyclooctanes: A previously unrecognized mechanism for acrolein-mediated oxidative stress

Acrolein, a toxic unsaturated aldehyde generated as a result of oxidative stress, readily reacts with a variety of nucleophilic biomolecules. Polyamines, which produced acrolein in the presence of amine oxidase, were then found to react with acrolein to produce 1,5-diazacyclooctane, a previously unrecognized but significant downstream product of oxidative stress. Although diazacyclooctane formation effectively neutralized acrolein toxicity, the diazacyclooctane hydrogel produced through a sequential diazacyclooctane polymerization reaction was highly cytotoxic. This study suggests that diazacyclooctane formation is involved in the mechanism underlying acrolein-mediated oxidative stress.

Hydrogenation of N-Heteroarenes Using Rhodium Precatalysts: Reductive Elimination Leads to Formation of Multimetallic Clusters

A rhodium-catalyzed method for the hydrogenation of N-heteroarenes is described. A diverse array of unsubstituted N-heteroarenes including pyridine, pyrrole, and pyrazine, traditionally challenging substrates for hydrogenation, were successfully hydrogenated using the organometallic precatalysts, [(η5-C5Me5)Rh(N-C)H] (N-C = 2-phenylpyridinyl (ppy) or benzo[h]quinolinyl (bq)). In addition, the hydrogenation of polyaromatic N-heteroarenes exhibited uncommon chemoselectivity. Studies into catalyst activation revealed that photochemical or thermal activation of [(η5-C5Me5)Rh(bq)H] induced C(sp2)-H reductive elimination and generated the bimetallic complex, [(η5-C5Me5)Rh(μ2,η2-bq)Rh(η5-C5Me5)H]. In the presence of H2, both of the [(η5-C5Me5)Rh(N-C)H] precursors and [(η5-C5Me5)Rh(μ2,η2-bq)Rh(η5-C5Me5)H] converted to a pentametallic rhodium hydride cluster, [(η5-C5Me5)4Rh5H7], the structure of which was established by NMR spectroscopy, X-ray diffraction, and neutron diffraction. Kinetic studies on pyridine hydrogenation were conducted with each of the isolated rhodium complexes to identify catalytically relevant species. The data are most consistent with hydrogenation catalysis prompted by an unobserved multimetallic cluster with formation of [(η5-C5Me5)4Rh5H7] serving as a deactivation pathway.