66937-52-8

Basic information

• Product Name: Glycine, N-(2-phenylethyl)-, 1,1-dimethylethyl ester
• CAS NO: 66937-52-8
• Molecular Formula: C14H21NO2
• Molecular Weight: 235.326
• Mol File: 66937-52-8.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: Glycine, N-(2-phenylethyl)-, 1,1-dimethylethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Glycine, N-(2-phenylethyl)-, 1,1-dimethylethyl ester(66937-52-8)
• EPA Substance Registry System: Glycine, N-(2-phenylethyl)-, 1,1-dimethylethyl ester(66937-52-8)

Safety Data

• Hazardous Substances Data: 66937-52-8(Hazardous Substances Data)

Upstream product

• 1336-21-6 ammonium hydroxide 
• 5292-43-3 bromoacetic acid tert-butyl ester 
• 64-04-0 phenethylamine 

Downstream Products

• 1427753-02-3 4-{2-[(2-tert-butoxy-2-oxoethyl)(2-phenylethyl)amino]-2-oxoethyl}-3-chlorophenyl 4-[N',N''-bis(tert-butoxycarbonyl)carbamimidamido]benzoate 
• 7738-38-7 2-(phenethylamino)acetic acid 
• 393155-75-4 (2S,4R)-4-Mercapto-1-(naphthalene-2-sulfonyl)-pyrrolidine-2-carboxylic acid phenethyl-amide 
• 84827-70-3 (S)-2-[(S)-1-(tert-Butoxycarbonylmethyl-phenethyl-carbamoyl)-ethylamino]-4-phenyl-butyric acid ethyl ester 

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.

Peptoids bearing tertiary amino residues in the n-alkyl side chains: synthesis of a potent inhibitor of Semaphorin 3A

A study on the preparation of N-alkylglycines (peptoids) that contain tertiary amino residues on the N-alkyl side chains is reported. The appropriate combination of the submonomer strategy with N-alkylglycine monomer couplings depending upon the structure of the N-alkyl side chain that must be incorporated into the peptoid is determinant for the efficiency of the synthetic pathway. The application of this strategy to the preparation of SICHI, an N-alkyglycine trimer containing tertiary amino residues in the three N-alkyl branches, and that has been identified as a potent Semaphorin 3A inhibitor, is presented.

Pyrrolidine derivatives

The present invention relates to pyrrolidine derivatives and dimeric forms and/or pharmaceutically acceptable esters, and/or salts thereof. The compounds are useful as inhibitors of metalloproteases, e.g. zinc proteases, particularly zinc hydrolases, and which are effective in treating disease states are associated with vasoconstriction of increasing occurrences.