19460-86-7Relevant articles and documents
Postsynthetic Modification of Phenylalanine Containing Peptides by C-H Functionalization
Terrey, Myles J.,Perry, Carole C.,Cross, Warren B.
supporting information, p. 104 - 108 (2019/01/11)
New methods for peptide modification are in high demand in drug discovery, chemical biology, and materials chemistry; methods that modify natural peptides are particularly attractive. A Pd-catalyzed, C-H functionalization protocol for the olefination of phenylalanine residues in peptides is reported, which is compatible with common amino acid protecting groups, and the scope of the styrene reaction partner is broad. Bidentate coordination of the peptide to the catalyst appears crucial for the success of the reaction.
Study of intramolecular aminolysis in peptides containing N-alkylamino acids at position 2
Ryakhovsky, Vladimir V.,Ivanov, Andrey S.
supporting information; experimental part, p. 7070 - 7076 (2012/08/29)
Many peptides and proteins, containing Nα-alkylamino acids (including proline) at the second position, are prone to intramolecular aminolysis (IA) with elimination of N-terminal dipeptide sequence as 2,5-diketopiperazines (DKP). We synthesized a series of short peptides, containing N-alkylamino acids at position 2, and studied their stability in the presence of acetic acid and amines. The presence of side chains in the second and the third amino acid residues and alkylation at Nα of the third amino acid residue slowed down IA. Nα-Alkyl residue in the first amino acid residue impeded IA only in peptides, containing three or more residues. Side chains of the first amino acids did not affect significantly the cleavage rates. Acetic acid promoted IA more strongly than aqueous ammonia, while tertiary amines were less effective. Peptides with methionine-S-oxide residues were more labile than the unoxidized analogs, suggesting intramolecular assistance of the S-oxide group in aminolysis. Surprisingly, intermediate compounds of the formula Boc-Met-MeXaa-Sar-NHR underwent rapid cleavage (endopeptolysis) upon attempted acidolytic deprotection.
Peptide Sweeteners. 3. Effect of Modifying the Peptide Bond on the Sweet Taste of L-Aspartyl-L-phenylalanine Methyl Ester and Its Analogues
MacDonald, Scott A.,Willson, C. Grant,Chorev, Michael,Vernacchia, Fred S.,Goodman, Murray
, p. 413 - 420 (2007/10/02)
A series of analogues designed to assess the importance of the amide bond in the dipeptide sweetener L-aspartyl-L-phenylalanine methyl ester has been synthesized and tested.The peptide bond was methylated, replaced by an ester bond, or reversed.All of the
Amino-acids and Peptides, Part 44. Synthesis of Protected Peptides related to Sequence 23-30 of Bovine Insulin B-Chain
Warnke, Jonathan G.,Young, Geoffrey T.
, p. 2797 - 2800 (2007/10/02)
Protected peptides related to the C-terminal octapeptide sequence (1) of the B-chain of bovine insulin, including those in which phenylalanine-24 and -25 have been replaced by alanine and by N-methylphenylalanine, have been synthesized by the picolyl este
