72150-35-7

Basic information

• Product Name: BZ-PHE-NH2
• Synonyms: N-ALPHA-BENZOYL-L-PHENYLALANINE AMIDE;BZO-PHE-NH2;BZ-PHE-NH2;BZ-PHENYLALANINE-NH2;BENZOYL-L-PHENYLALANINE AMIDE;Bz-L-Phe-NH2;N-α-Benzoyl-L-phenylalanine amide;Na-Benzoyl-L-phenylalanine amide≥ 99% (TLC)
• CAS NO: 72150-35-7
• Molecular Formula: C₁₆H₁₆N₂O₂
• Molecular Weight: 268.31
• Product Categories: Amino Acid Derivatives;Amino Acids
• Mol File: 72150-35-7.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• Storage Temp.: Store at RT.
• CAS DataBase Reference: BZ-PHE-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: BZ-PHE-NH2(72150-35-7)
• EPA Substance Registry System: BZ-PHE-NH2(72150-35-7)

Safety Data

• Hazardous Substances Data: 72150-35-7(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Upstream product

• 3005-61-6 methyl (S)-2-(benzoylamino)-3-phenylpropanoate 
• 98-88-4 benzoyl chloride 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 1394992-03-0 C₃₁H₃₀N₂O₄ 
• 2566-22-5 N-benzoyl-L-phenylalanine 
• 131458-24-7 Bz-Phe-Ser-OMe 
• 131458-30-5 Bz-Phe-Thr-OMe 
• 1394992-02-9 C₂₅H₂₆N₂O₄ 
• 1394992-01-8 C₂₆H₂₈N₂O₅ 
• 143573-04-0 C₂₅H₂₆N₂O₄ 

Downstream Products

• 142066-11-3 N-Benzoyl-L-thiophenylalanin-O-ethylester 

Relevant articles and documents

Identification of 1,5,7-Triazabicyclododecene and Polystyrene-Supported Superbases as Efficient Hydroxylaminolysis Agents of Sterically Hindered and Epimerizable Esters

In modern pharmaceutical research, the need for reliable protocols for the preparation of chemical libraries in a controlled manner is quintessential to driving the Design-Make-Test cycle in drug discovery programs. In this letter, we communicate the iden

Protein backbone modification by novel C(α)-C side-chain scission

α-Ketoamide (-NH-CO-CO-) units in intact peptides are generated from Ser/Thr residues via Ru(VIII)-catalyzed C(α)-C side-chain scission. Facets associated with this novel α-carbon modification have been probed with 75 peptides chosen to represent every possible peptide environment. The reactions were carried out at room temperature with in situ generated Ru(VIII) in biphasic (CH3CN/CCl4/pH 3 phosphate buffer, 1:1:2 v/v) medium. Whereas Ser/Thr residues placed at the C-terminal end in peptides undergo N-C bond scission leading to des-Ser/Thr peptide amides - thus acting as Gly equivalents in simulating the α-amidating action of pituitary enzymes - those located at the N-terminal or nonterminal or even at the C-terminal position (protected as amide) were found to undergo oxidative C-C bond scission (involving C(α) and C side-chain bond), resulting in the generation of α-ketoamide (-NH-CO-CO-) units in the intact peptide backbone. The difference in the products arising from C(α)-C side-chain scission of Ser/Thr esters and amides is rationalized on the basis of a common mechanism involving either oxaloesters [PeP-NH-CO-COX; X = OMe] or oxalamides [X = NH2 or NH-Pep] arising from the oxidation of initially formed carbinolamide intermediates [Pep-NH-CH(OH)-COX], wherein, while the former are shown to undergo hydrolysis to terminal amides [Pep-NH2], the oxalamides are found to be stable to hydrolysis. Ancillary noteworthy findings are those of peptide bond scission when contiguous Ser-Ser/Thr-Thr residues are present and the oxidative cleavage at C-terminal Tyr/Trp sites generating des amides. The oxidative methodology presented here is mild, simple, and practical and proceeds with chiral retention. The insensitivity of a large number of amino acid residues, such as Gly, Ala, Leu, Asn, Gln, Asp, Glu, Pro, Arg, Phe, Lys, Val, and Aib, and N-protecting groups, such as Boc, Z, and Bz, toward Ru(VIII) under the experimental conditions should make this methodology practical and useful. Sulfur-containing amino acids Cys and Met get oxidized to sulfones in the products.