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.
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