258332-57-9

Basic information

• Product Name: N-[3-(BOC-AMINO)PROPYL]GLYCINE ETHYL ESTER
• Synonyms: N-[3-(TERT-BUTOXYCARBONYLAMINO)PROPYL]GLYCINE ETHYL ESTER;N-[3-(BOC-AMINO)PROPYL]GLYCINE ETHYL ESTER;N-[3-(tert-Butoxycarbonylamino)propyl]glycine Ethyl Ester;Ethyl 2-((3-((tert-butoxycarbonyl)
• CAS NO: 258332-57-9
• Molecular Formula: C₁₂H₂₄N₂O₄
• Molecular Weight: 260.33
• Mol File: 258332-57-9.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 368.903°C at 760 mmHg
• Flash Point: 176.907°C
• Appearance: /
• Density: 1.036g/cm³
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.4550-1.4590
• Storage Temp.: Refrigerator
• PKA: 12.77±0.46(Predicted)
• CAS DataBase Reference: N-[3-(BOC-AMINO)PROPYL]GLYCINE ETHYL ESTER(CAS DataBase Reference)
• NIST Chemistry Reference: N-[3-(BOC-AMINO)PROPYL]GLYCINE ETHYL ESTER(258332-57-9)
• EPA Substance Registry System: N-[3-(BOC-AMINO)PROPYL]GLYCINE ETHYL ESTER(258332-57-9)

Safety Data

• Hazardous Substances Data: 258332-57-9(Hazardous Substances Data)

Usage

General Description

N-[3-(BOC-AMINO)PROPYL]GLYCINE ETHYL ESTER is a chemical compound commonly used as a reagent in organic synthesis. It is an ethyl ester derivative of N-[3-(BOC-amino)propyl]glycine, which is a protected form of the amino acid glycine. The BOC group (tert-butyloxycarbonyl) is a common protecting group used to temporarily mask the amine functionality of amino acids to prevent unwanted reactions during chemical synthesis. N-[3-(BOC-AMINO)PROPYL]GLYCINE ETHYL ESTER is often utilized in the production of peptides and pharmaceuticals, as well as in other areas of organic chemistry research. Its use allows for the selective modification of amino acids and the synthesis of complex molecules with specific structural features.

InChI:InChI=1/C12H24N2O4/c1-5-17-10(15)9-13-7-6-8-14-11(16)18-12(2,3)4/h13H,5-9H2,1-4H3,(H,14,16)

Upstream product

• 75178-96-0 N-Boc-1,3-diaminopropane 
• 105-36-2 ethyl bromoacetate 
• 24424-99-5 di-tert-butyl dicarbonate 
• 105-39-5 chloroacetic acid ethyl ester 

Downstream Products

• 367955-16-6 {N-[3-(tert-Butoxycarbonylamino)propyl]-N-(pentafluorobenzoyl)amino}acetic acid ethyl ester 
• 367955-18-8 {N-[3-(tert-Butoxycarbonylamino)propyl]-N-(2,4-difluoro-5-methylbenzoyl)amino}acetic acid ethyl ester 
• 192124-66-6 N,N'-bis(tert-butoxycarbonyl)-(3-aminopropyl)-glycine 
• 352285-28-0 (R)-[2-(3-Amino-propylamino)-acetoxy]-phenyl-acetic acid methyl ester 
• 352285-41-7 {3-[({[benzofuran-2-yl-(4-chloro-phenyl)-methyl]-carbamoyl}-methyl)-tert-butoxycarbonyl-amino]-propyl}-carbamic acid tert-butyl ester 
• 352285-39-3 {3-[tert-butoxycarbonyl-({[(1-methanesulfonyl-1H-indol-2-yl)-m-tolyl-methyl]-carbamoyl}-methyl)-amino]-propyl}-carbamic acid tert-butyl ester 
• 143192-31-8 N-(((9H-fluoren-9-yl)methoxy)carbonyl)-N-(5-((tert-butoxycarbonyl)amino)propyl)glycine 

Relevant articles and documents

Peptide/peptoid hybrid oligomers: The influence of hydrophobicity and relative side-chain length on antibacterial activity and cell selectivity

Previous optimisation studies of peptide/peptoid hybrids typically comprise comparison of structurally related analogues displaying different oligomer length and diverse side chains. The present work concerns a systematically constructed series of 16 closely related 12-mer oligomers with an alternating cationic/hydrophobic design, representing a wide range of hydrophobicity and differences in relative side-chain lengths. The aim was to explore and rationalise the structure-activity relationships within a subclass of oligomers displaying variation of three structural features: (i) cationic side-chain length, (ii) hydrophobic side-chain length, and (iii) type of residue that is of a flexible peptoid nature. Increased side-chain length of cationic residues led to reduced hydrophobicity till the side chains became more extended than the aromatic/hydrophobic side chains, at which point hydrophobicity increased slightly. Evaluation of antibacterial activity revealed that analogues with lowest hydrophobicity exhibited reduced activity against E. coli, while oligomers with the shortest cationic side chains were most potent against P. aeruginosa. Thus, membrane-disruptive interaction with P. aeruginosa appears to be promoted by a hydrophobic surface of the oligomers (comprised of the aromatic groups shielding the cationic side chains). Peptidomimetics with short cationic side chains exhibit increased hemolytic properties as well as give rise to decreased HepG2 (hepatoblastoma G2 cell line) cell viability. An optimal hydrophobicity window could be defined by a threshold of minimal hydrophobicity conferring activity toward E. coli and a threshold for maximal hydrophobicity, beyond which cell selectivity was lost.

Chiral recognition by CD-sensitive dimeric zinc porphyrin host. 1. Chiroptical protocol for absolute configurational assignments of monoalcohols and primary monoamines

A general microscale protocol for the determination of absolute configurations of primary amino groups or secondary hydroxyl groups linked to a single stereogenic center is described. The chiral substrates are linked to the achiral trifunctional bidentate carrier molecule (3-aminopropylamino)acetic acid (1, H2NCH2CH2CH2NHCH2COOH) and the resultant conjugates are then complexed with dimeric zinc porphyrin host 2 giving rise to 1:1 host/guest sandwiched complexes. These complexes exhibit exciton-coupled bisignate CD spectra due to stereodifferentiation leading to preferred porphyrin helicity. Since the chiral sense of twist between the two porphyrins in the complex is dictated by the stereogenic center of the substrate, the sign of the couplet determines the absolute configuration at this center. The twist of the porphyrin tweezer in the complex can be predicted from the relative steric sizes of the groups flanking the stereogenic center, such that the bulkier group protrudes from the complex sandwich. In certain α-hydroxy esters and α-amino esters, electronic factors and hydrogen bonding govern the preferred conformation of the complex, and hence the CD spectra.