205807-93-8Relevant academic research and scientific papers
Postsynthetic Modification of Phenylalanine Containing Peptides by C-H Functionalization
Terrey, Myles J.,Perry, Carole C.,Cross, Warren B.
, p. 104 - 108 (2019)
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.
Interkingdom pharmacology of angiotensin-I converting enzyme inhibitor phosphonates produced by actinomycetes
Kramer, Glenna J.,Mohd, Akif,Schwager, Sylva L. U.,Masuyer, Geoffrey,Acharya, K. Ravi,Sturrock, Edward D.,Bachmann, Brian O.
supporting information, p. 346 - 351 (2014/05/06)
The K-26 family of bacterial secondary metabolites are N-modified tripeptides terminated by an unusual phosphonate analog of tyrosine. These natural products, produced via three different actinomycetales, are potent inhibitors of human angiotensin-I converting enzyme (ACE). Herein we investigate the interkingdom pharmacology of the K-26 family by synthesizing these metabolites and assessing their potency as inhibitors of both the N-terminal and C-terminal domains of human ACE. In most cases, selectivity for the C-terminal domain of ACE is displayed. Co-crystallization of K-26 in both domains of human ACE reveals the structural basis of the potent inhibition and has shown an unusual binding motif that may guide future design of domain-selective inhibitors. Finally, the activity of K-26 is assayed against a cohort of microbially produced ACE relatives. In contrast to the synthetic ACE inhibitor captopril, which demonstrates broad interkingdom inhibition of ACE-like enzymes, K-26 selectively targets the eukaryotic family.
