7298-84-2Relevant articles and documents
AGRICULTURAL PLANT-PROTECTING AGENTS CONTAINING DIPEPTIDE DERIVATIVE AS ACTIVE INGREDIENT
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Paragraph 0122; 0123, (2015/05/05)
Provided is an agricultural plant-protecting agent including a dipeptide derivative or an agro-pharmaceutically acceptable salt thereof as an active ingredient, which has a plant disease-preventing effect, a plant growth-promoting effect, and a plant immunity-activating effect.
Compositions and Methods for Binding Lysophosphatidic Acid
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, (2009/06/27)
Compositions and methods for making and using anti-LPA agents, for example, monoclonal antibodies, are described.
Molecular recognition of l-leucyl-l-alanine: Enantioselective inclusion of alkyl methyl sulfoxides
Akazome, Motohiro,Hirabayashi, Atsushi,Takaoka, Kousuke,Nomura, Satoru,Ogura, Katsuyuki
, p. 1107 - 1113 (2007/10/03)
A simple aliphatic dipeptide, l-leucyl-l-alanine (Leu-Ala), includes several alkyl methyl sulfoxides enantioselectively to form inclusion crystals. From single-crystal X-ray analyses of three inclusion compounds of dimethyl sulfoxide (DMSO), isobutyl methyl sulfoxide, and benzyl methyl sulfoxide, it was elucidated that Leu-Ala molecules self-assemble to form layer structures and the sulfoxides are included via hydrogen bonding in a cavity between these layers. The inclusion cavity has methyl group and isobutyl group at its each side, and the guest sulfoxide is placed in such a manner that its methyl group faces toward the methyl of the Leu-Ala cavity. When the alkyl group of the sulfoxide is comparably large, it is located in the residual space of the cavity to attain effective crystal packing. Thus, the sulfoxides having a comparably large group such as isobutyl, butyl, and benzyl are included with a high (R)-enantioselectivity in Leu-Ala crystals.
An expedient N-terminal attachment methodology for the solid phase peptide synthesis
Li,Sung Tsai Lin,Jian Hsiu Yang
, p. 1608 - 1612 (2007/10/03)
A general and successful N-terminal attachment methodology is described that allows the solid phase synthesis of oligopeptides from activated N-hydroxysuccinimide esters and amino acid lithium salts. The results of studies with different coupling systems for amide bond formation are presented. The oligomers were synthesized on solid support using a carbamate linker with final TFA/CH2Cl2 cleavage. This methodology was also applied for the preparation of peptide-substituted amides and esters in high purities and excellent yields.
Rates of reduction of N-chlorinated peptides by sulfite: Relevance to incomplete dechlorination of wastewaters
Jensen, James S.,Helz, George R.
, p. 516 - 522 (2007/10/03)
Biologically induced fragmentation of proteins during wastewater treatment produces peptides, which form long-lasting organic chloramines when the water is disinfected with Cl2. To protect aquatic wildlife from residual chlorine, including chloramines, wastewaters are often treated with sulfur dioxide or sulfite salts. This strategy incompletely eliminates residual chlorine species. Here we report that dechlorination rate constants of N- chloropeptides are 1-2 orders of magnitude smaller than those for NH2Cl and some aliphatic organic chloramines. Slow rates explain the prevalence of N- chloropeptides in dechlorinated wastewaters after faster reacting chlorine species have been eliminated. Dechlorination is subject to general acid catalysis. For N-chlorinated leucylalanine, the rate law above pH 6 in phosphate buffer at 25 °C and / ? 0.1 M is as follows: rate = (9.92 ± 0.41 x 103[H2PO4-] + 5.70 ± 0.52 x 108[H3O+] + 5.3 ± 0.2)[SO32-][Cl- Leu-Ala] (concentrations in M, time in s). Rate constants for other peptides appear to be of similar magnitude; variations in the acid-catalyzed terms among different hydrophobic peptides correlate with solvation energies of side chains. The kinetic data suggest that reducing N-chloropeptides in wastewaters by 75% or more will require reaction times generally >0.5 h at environmentally acceptable S(IV) doses and pH values. Biologically induced fragmentation of proteins during wastewater treatment produces peptides, which form long-lasting organic chloramines when the water is disinfected with Cl2. To protect aquatic wildlife from residual chlorine, including chloramines, wastewaters are often treated with sulfur dioxide or sulfite salts. This strategy incompletely eliminates residual chlorine species. Here we report that dechlorination rate constants of N-chloropeptides are 1-2 orders of magnitude smaller than those for NH2Cl and some aliphatic organic chloramines. Slow rates explain the prevalence of N-chloropeptides in dechlorinated wastewaters after faster reacting chlorine species have been eliminated. Dechlorination is subject to general acid catalysis. For N-chlorinated leucylalanine, the rate law above pH 6 in phosphate buffer at 25 °C and I≈0.1 M is as follows: rate = (9.92±0.41×103[H2 PO4- ]+5.70±0.52×108[ H3O+]+5.3±0.2) [SO32-][Cl-Leu-Ala] (concentrations in M, time in s). Rate constants for other peptides appear to be of similar magnitude; variations in the acid-catalyzed terms among different hydrophobic peptides correlate with solvation energies of side chains. The kinetic data suggest that reducing N-chloropeptides in wastewaters by 75% or more will require reaction times generally >0.5 h at environmentally acceptable SIV doses and pH values.
Role of basic and acidic fragments in delicious peptides (Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) and the taste behavior of sodium and potassium salts in acidic oligopeptides.
Nakata,Takahashi,Nakatani,Kuramitsu,Tamura,Okai
, p. 689 - 693 (2007/10/02)
The role of the acidic fragment (Asp-Glu-Glu) in delicious peptides was investigated in detail by using the Na+ or K+ salts of acidic oligopeptides so that amount of Na+ or K+ intake of peptides composed of acidic amino acids could be varied by changing their sequences. The taste of these peptides was confirmed to vary with Na+ or K+ intake. Additionally, in order to study the role of basic (Lys-Gly) and acidic (Asp-Glu-Glu) fragments in delicious peptides for producing the taste, five delicious peptide analogs, Ser-Leu-Ala-Lys-Gly-Asp-Glu-Glu, Ser-Leu-Ala-Asp-Glu-Glu-Lys-Gly, Lys-Gly-Ser-Leu-Ala-Asp-Glu-Glu, Lys-Gly-Asp-Glu-Glu, and Glu-Glu-Asp-Gly-Lys, were synthesized. The intensity of the umami and/or salty taste of these peptides and their Na salts was almost the same, despite their chemical structures being different. These results indicate that the acidic fragment as well as the basic fragment plays an important role in the taste production and intensity of delicious peptides, and that an umami or salty taste can be produced by the localization of the cation of the basic fragment and the anion of the acidic fragment.
Catalytic properties of X-prolyl dipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris nTR.
Yan,Ho,Hou
, p. 704 - 707 (2007/10/02)
An X-prolyl dipeptidyl aminopeptidase (X-PDAP; EC 3.4.14.5) was identified to be loosely bound on the inner cell membrane fraction of Lactococcus lactis subsp. cremoris nTR. The biosynthesis of X-PDAP was continuously increased before the late-log growth phase of the bacteria. Both Gly-Pro-pNA and Ala-Ala-pNA were hydrolyzed by X-PDAP; the kcat/Km value of the former was about 10-fold that of the latter. The Ki of X-Pro and Pro-X were more specific to X-PDAP than those of X-Ala. The enzyme splitting a dipeptide sequentially from beta-casomorphin as a model catalytic pattern was identified and some properties of the enzyme were further characterized.
The Steric Hindrance of the Stepwise Reaction of N-Carboxy α-Amino Acid Anhydride with the α-Amino Acid Ester
Oya, Masanao,Takahashi, Tomoko
, p. 2705 - 2707 (2007/10/02)
The mechanisms of the reactions of 4-alkyloxazolidinediones (1) (N-carboxy α-amino acid anhydrides(NCAs)) with α-amino acid benzyl ester p-toluenesulfonates (2) were investigated in acetonitrile containing triethylamine at low and room temperatures.Two types of reactions were observed: (1) the polymerization of NCAs was initiated with a small amount of 2 to produce polypeptides (6), and (2) the dipeptide benzyl esters (4) were produced by the stepwise reaction of NCAs with the esters.Both the polymerization and the dipeptide formation (1+2) seemed to be initiated by the nucleophilic attack of the amino group of the ester on the C-5 carbon of NCAs.The polymerization proceeded when the side chains of the amino acid esters (R2) were more bulky than those of the NCAs (R1).On the contrary, dipeptide esters were produced when the side chains of the NCAs (R1) were more bulky than those of the esters (R2).
Peptides 119. - Peptide Synthesis with N-Carboxy-α-amino Acid Anhydrides
Kircher, K.,Berndt, H.,Zahn, H.
, p. 275 - 284 (2007/10/02)
On reaction of N-carboxy-α-amino acid anhydrides (NCA) with equimolar amounts of aminoacids or excess NCA in potassium borate buffer of pH 10.2 (0 deg C) considerable amounts of homooligomers and homopolymers are formed.If an excess of amino acid is used formation of the above mentioned by-products can be suppressed.The extent of homooligomerization and homopolymerization and hydrolysis occurring during the reaction of NCA under the conditions of peptide synthesis is described.
