Inside Cover: Peptide Backbone Composition and Protease Susceptibility: Impact of Modification Type, Position, and Tandem Substitution (ChemBioChem 8/2016). (5th April 2016)

• Record Type: Journal Article
• Authors: Werner, Halina M.; Cabalteja, Chino C.; Horne, W. Seth
• Is Part Of: Chembiochem. Volume 17:Number 8(2016)
• Page Start: 643
• Page End: 643
• Publication Date: 2016-04-05
• Subjects: peptides -- foldamers -- peptidomimetics -- proteases -- protein–protein interactions; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201600145
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract : The inside cover picture shows the hydrolysis of a polypeptide substrate by a protease enzyme (top) and the interruption of this process through the incorporation of unnatural units in the substrate backbone (bottom). Comparison of the proteolytic resistance imparted as a function of modification type, position, and tandem substitution reveal how the magnitude and sphere of protection vary with backbone chemical composition. These results promise to aid in the design of biostable mimics of peptides and proteins with complex folding patterns. More information can be found in the full paper by W. S. Horne et al. onpage 712 in Issue 8, 2016 (DOI:10.1002/cbic.201500312 ).