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Tert-butyl 5-aminopentanoate is a chemical compound that features a 5-aminopentanoate group attached to a tert-butyl group. It is widely recognized for its role in organic synthesis and its potential applications in the development of pharmaceuticals and biologically active compounds. Its antimicrobial and antifungal properties have garnered interest for its use in creating new drugs and treatments. Furthermore, its low toxicity and stable nature contribute to its reputation as a safe and versatile chemical for research and industrial applications.

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  • 63984-03-2 Structure
  • Basic information

    1. Product Name: tert-butyl 5-aminopentanoate
    2. Synonyms: tert-butyl 5-aminopentanoate;5-Aminopentanoic acid tert-butyl ester
    3. CAS NO:63984-03-2
    4. Molecular Formula: C9H19NO2
    5. Molecular Weight: 173.25266
    6. EINECS: N/A
    7. Product Categories: N/A
    8. Mol File: 63984-03-2.mol
  • Chemical Properties

    1. Melting Point: N/A
    2. Boiling Point: 220.1±23.0 °C(Predicted)
    3. Flash Point: N/A
    4. Appearance: /
    5. Density: 0.940±0.06 g/cm3(Predicted)
    6. Refractive Index: N/A
    7. Storage Temp.: Keep in dark place,Inert atmosphere,Store in freezer, under -20°C
    8. Solubility: N/A
    9. PKA: 10.27±0.10(Predicted)
    10. CAS DataBase Reference: tert-butyl 5-aminopentanoate(CAS DataBase Reference)
    11. NIST Chemistry Reference: tert-butyl 5-aminopentanoate(63984-03-2)
    12. EPA Substance Registry System: tert-butyl 5-aminopentanoate(63984-03-2)
  • Safety Data

    1. Hazard Codes: N/A
    2. Statements: N/A
    3. Safety Statements: N/A
    4. WGK Germany:
    5. RTECS:
    6. HazardClass: N/A
    7. PackingGroup: N/A
    8. Hazardous Substances Data: 63984-03-2(Hazardous Substances Data)

63984-03-2 Usage

Uses

Used in Pharmaceutical Industry:
Tert-butyl 5-aminopentanoate is utilized as a reagent for the synthesis of various pharmaceuticals due to its ability to facilitate the creation of biologically active compounds.
Used in Antimicrobial and Antifungal Applications:
In the field of microbiology, tert-butyl 5-aminopentanoate is employed as an antimicrobial and antifungal agent, leveraging its natural properties to combat infections and develop new treatments.
Used in Research and Development:
Tert-butyl 5-aminopentanoate is used as a key component in research and development for its low toxicity and stable nature, making it an ideal candidate for exploring new chemical reactions and applications in various industries.

Check Digit Verification of cas no

The CAS Registry Mumber 63984-03-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,3,9,8 and 4 respectively; the second part has 2 digits, 0 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 63984-03:
(7*6)+(6*3)+(5*9)+(4*8)+(3*4)+(2*0)+(1*3)=152
152 % 10 = 2
So 63984-03-2 is a valid CAS Registry Number.

63984-03-2SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name δ-aminovaleric acid tert-butyl ester

1.2 Other means of identification

Product number -
Other names 5-aminovaleric acid tert.-butyl ester

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:63984-03-2 SDS

63984-03-2Relevant articles and documents

SUBSTITUTED 2,3-BENZODIAZEPINES DERIVATIVES

-

Page/Page column 53, (2021/08/06)

Derivatives of 2,3- benzodiazepines as inhibitors of Bromodomain and extra C-terminal domain (BET) proteins, in particular the BRD4 family member, methods of preparing said compounds, intermediate compounds useful for preparing said compounds, pharmaceuti

Optimized reaction pair of the Cyshis tag and Ni(II)-Nta probe for highly selective chemical labeling of membrane proteins

Zenmyo, Naoki,Tokumaru, Hiroki,Uchinomiya, Shohei,Fuchida, Hirokazu,Tabata, Shigekazu,Hamachi, Itaru,Shigemoto, Ryuichi,Ojida, Akio

supporting information, p. 995 - 1000 (2019/07/18)

Chemical labeling of proteins with synthetic molecular probes offers the possibility to probe the functions of proteins of interest in living cells. However, the methods for covalently labeling targeted proteins using complementary peptide tag-probe pairs are still limited, irrespective of the versatility of such pairs in biological research. Herein, we report the new CysHis tag-Ni(II) probe pair for the specific covalent labeling of proteins. A broad-range evaluation of the reactivity profiles of the probe and the CysHis peptide tag afforded a tag-probe pair with an optimized and high labeling selectivity and reactivity. In particular, the labeling specificity of this pair was notably improved compared to the previously reported one. This pair was successfully utilized for the fluorescence imaging of membrane proteins on the surfaces of living cells, demonstrating its potential utility in biological research.

Heterovalent inhibitors targeting N-end Rule Pathway and its use

-

, (2016/10/10)

An alkali-soluble polymer resin compound of formula 1 a including N-end Rule pathway inhibitors disclosure the composition. According to type 1 and type 2 herein each compounds recognizing substrate UBR box and a ClpS box a mammal having two tolerance N-e

Synthesis and self-association properties of flexible guanidiniocarbonylpyrrole-carboxylate zwitterions in DMSO: Intra- versus intermolecular ion pairing

Schmuck, Carsten,Rehm, Thomas,Geiger, Lars,Schaefer, Mathias

, p. 6162 - 6170 (2008/02/10)

(Chemical Equation Presented) We have synthesized a new class of flexible zwitterions 6a-e, in which a carboxylate is linked via an alkyl chain with variable length (one to five methylene groups) to a guanidiniocarbonylpyrrole cation. The self-association properties of these zwitterions were determined by NMR dilution studies in DMSO and by ESI-MS experiments. The stability and hence also the size of the aggregates formed via self-assembly is critically dependent on the length and therefore flexibility of the spacer. Whereas the smallest zwitterion 6a forms large aggregates already at low concentrations, the more flexible zwitterions only form small oligomers (6b) or dimers (6c-e) at much larger concentrations. The differences between the five zwitterions can be explained based on the different extent of intramolecular ion pairing within the monomers. Any intramolecular ion pairing, which becomes possible with increasing linker length, stabilizes the monomer and therefore destabilizes any oligomer.

Building Units for N-Backbone Cyclic Peptides. 3. Synthesis of Protected Nα-(ω-Aminoalkyl)amino Acids and Nα-(ω-Carboxyalkyl)amino Acids

Muller, Dan,Zeltser, Irena,Bitan, Gal,Gilon, Chaim

, p. 411 - 416 (2007/10/03)

An improved synthesis of a family of amino acids that contain ω-aminoalkyl groups and of a new family containing ω-carboxyalkyl groups linked to the α-amine is described. The synthesis was performed by alkylation of suitably monoprotected alkylenediamines and protected ω-amino acids with triflates of α-hydroxy acid esters. The reaction proceeded with inversion of configuration yielding optically pure products. The Nα-(ω-aminoalkyl)amino acids and Nα-(ω-carboxyalkyl)amino acids were orthogonally protected to allow their incorporation into peptides by solid-phase peptide synthesis (SPPS) methodology.

New kelatorphan-related inhibitors of enkephalin metabolism: Improved antinociceptive properties

Xie,Soleilhac,Schmidt,Peyroux,Roques,Fournie-Zaluski

, p. 1497 - 1503 (2007/10/02)

In order to improve the in vivo protection of enkephalins from enzymatic degradation, a new series of inhibitors derived from kelatorphan [HONHCOCH2CH(CH2Ph)CONHCH(CH3)COOH], the first-described complete inhibitor of enkephalin metabolism, were designed by modification of the C-terminal amino acid. The progressive lengthening of the chain of this residue shows that a β-alanine seems to be the best basic model for the conception of such types of compounds. On the other hand, the methylation of the amide bond, which is well accepted by aminopeptidase N (EC 3.4.11.2) and dipeptidylaminopeptidase, induced a significant loss of affinity for neutral endopeptidase -24.11. Starting from these data, compounds containing a variously substituted β-alanine residue and corresponding to the general formula HONHCOCH2CH(CH2Ph)CONHCH(R1)CH(R2)COOH were synthesized. All these molecules inhibit neutral endopeptidase -24.11 and dipeptidylaminopeptidase in the nanomolar range, and those containing an aromatic chain (compound 7A, R1 = CH2Ph,R2 = H, and compound 8A, R1 = Ph, R2 = H) inhibit the biologically relevant aminopeptidase N, with IC50's around 10-8 M. Intracerebroventricular injection in mice of these multienzyme inhibitors produced an efficient and naloxone-reversible analgesic response (hot plate test): compounds 7A and 8A were shown to be more potent than kelatorpohan in increasing the jump latency time, in agreement with their in vitro properties, and these new compounds were found to increase the forepaw lick latency, a reflex considered as a typical morphine response.

SUBSTITUTED 5-AMINO-4-HYDROXYVALERYL DERIVATIVES

-

, (2008/06/13)

Compounds of the formula STR1 in which R 1 represents hydrogen or acyl, X 1 represents an optionally N-alkylated amino acid residue that is bonded N-terminally to R 1 and C-terminally to X 2, X 2 represents an optionally N-alkylated amino acid residue tha

Antibacterial halogenoacetyl derivatives of amino acids and simple peptides

Goodacre,Jeffries,Nayler,Ponsford,Stirling

, p. 1445 - 1448 (2007/10/12)

The vital role of D-alanine and L-lysine in the peptidoglycan crosslinking process in the bacterial cell wall prompted preparation of various small peptides incorporating these amino acids. N-Iodoacetyl or -bromoacetyl derivatives of the peptides were then prepared in the hope that they would serve as active-site-directed irreversible inhibitors of cell wall transpeptidases. Certain of the halogenoacetyl dipeptide esters, but not the corresponding free acids, showed slight antistaphylococcal activity. Subsequent structural variation showed that inclusion of D-alanine or L-lysine was not necessary, since antibacterial activity was at least as good when the dipeptide unit was replaced by glycylglycine or by an ω-aminoalkanoic acid. It was concluded that the observed antibacterial activity was probably not due to specific inhibition of a cell wall transpeptidase.

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