Functionalization of peptides and proteins by aldehyde or keto groups

• Published in: BIOPOLYM Vol. 55; no. 2; pp. 165 - 186
• Main Authors: Melnyk, Oleg, Fehrentz, Jean-Alain, Martinez, Jean, Gras-Masse, Hélène
• Format: Journal Article
• Language: English
• Published: New York John Wiley & Sons, Inc 2000; Wiley
• Subjects: Aldehydes; Aldehydes - chemistry; Chemical bonds; chemical ligation; Chemical modification; Chemical Sciences; Enzyme inhibition; Formic Acid Esters; hydrazone; Ketones - chemistry; Organic chemistry; oxazolidine; oxime; peptide aldehydes; Peptides - chemical synthesis; Proteins; Proteins - chemical synthesis; pseudoproline; Resins, Plant; solid phase; Synthesis (chemical); thiazolidine
• ISSN: 0006-3525; 1097-0282
• DOI: 10.1002/1097-0282(2000)55:2<165::AID-BIP50>3.0.CO;2-#

The functionalization of peptides and proteins by aldehyde or keto groups has become the subject of intensive research since the discovery of the inhibition properties of peptide aldehydes and the advent of protein engineering. The first part of this review focuses upon the tremendous efforts devoted to the solid‐phase synthesis of peptide aldehydes as protease inhibitors. The second part describes the utility of the aldehyde or keto functionalities for the site‐specific modification of peptides or proteins. © 2000 John Wiley & Sons, Inc. Biopoly 55: 165–186, 2000