98714-71-7

Basic information

• Product Name: Alanine, 2-methyl-N-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester
• CAS NO: 98714-71-7
• Molecular Formula: C22H26N2O5
• Molecular Weight: 398.459
• Mol File: 98714-71-7.mol
• Article Data: 8

Chemical Properties

• CAS DataBase Reference: Alanine, 2-methyl-N-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Alanine, 2-methyl-N-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester(98714-71-7)
• EPA Substance Registry System: Alanine, 2-methyl-N-[N-[(phenylmethoxy)carbonyl]-L-phenylalanyl]-, methyl ester(98714-71-7)

Safety Data

• Hazardous Substances Data: 98714-71-7(Hazardous Substances Data)

Upstream product

• 41518-17-6 Z-Phe-O-COO-isoBu 
• 15028-41-8 methyl 2-aminoisobutyrate hydrochloride 
• 13257-67-5 2-amino-2-methylpropionic acid methyl ester 
• 73048-81-4 benzyl (S)-(1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 501-53-1 benzyl chloroformate 
• 63-91-2 L-phenylalanine 
• 1161-13-3 N-Cbz-L-Phe 
• 769922-77-2 (S)-benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 

Downstream Products

• 109772-33-0 N-benzyloxycarbonyl-L-phenylalanyl-2-methylalanine 
• 143868-66-0 Z-Trp-Aib-Phe-Aib-Trp-Aib-Trp-Glyol 
• 143868-65-9 H-Trp-Aib-Phe-Aib-Trp-Aib-Trp-Glyol 
• 143868-68-2 Z-Phe-Aib-Trp-Aib-Trp-Glyol 
• 143868-67-1 H-Phe-Aib-Trp-Aib-Trp-Glyol 

Relevant articles and documents

Iodine-Mediated Oxidative Coupling of Hydroxamic Acids with Amines towards a New Peptide-Bond Formation

An efficient and straightforward approach for the coupling of Nα-protected hydroxamic acids with an amino component in the presence of iodine is delineated. The reaction is mediated by the formation of unstable but reactive acyl nitroso intermediates. The peptide hydroxamic acids were found to be useful substrates in coupling reactions.

Efficient peptide coupling involving sterically hindered amino acids

(Chemical Equation Presented) Hindered amino acids have been introduced into peptide chains by coupling N-(Cbz- and Fmoc-α-aminoacyl) benzotriazoles with amino acids, wherein at least one of the components was sterically hindered, to provide compounds 3a-e, (3c +3 c′), 5a-d, (5a + 5a′), 6a-c, (6b + 6b′), 8a-c, 9a-e, 10a-d, and (10a + 10a′) in isolated yields of 41-95% with complete retention of chirality as evidenced by NMR and HPLC analysis. The benzotriazole activation methodology is a new route for the synthesis of sterically hindered peptides. (Note: compound numbers written within brackets represent diastereomeric mixtures or racemates; compound numbers without brackets represent enantiomers.)

Relationship between the hydrophobicity of dipeptides and the Michaelis-Menten constant Km of their hydrolysis by carboxypeptidase-Y and carboxypeptidase-A

The enzymatic hydrolysis of dipeptides by carboxypeptidase-Y and carboxypeptidase-A was investigated. In the enzymatic hydrolysis of the dipeptides, a good linear relationship (r = 0.997 and 0.999) was found between the Michaelis-Menten constant (Km) and the hydrophobicity of the substrates evaluated from relative elution volume in reversed-phase HPLC. The correlation suggests that the hydrophobicity of the C-terminal amino acid is a major factor in governing the stability of the enzyme-substrate complex. The difference in the slope of the linear-regression lines seems to reflect the degree of relative hydrophobicity of the binding pockets in carboxypeptidase-Y and carboxypeptidase-A.