Premium
Inside Cover: Peptide Backbone Composition and Protease Susceptibility: Impact of Modification Type, Position, and Tandem Substitution (ChemBioChem 8/2016)
Author(s) -
Werner Halina M.,
Cabalteja Chino C.,
Horne W. Seth
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600145
Subject(s) - protease , tandem , chemistry , folding (dsp implementation) , peptide , substrate (aquarium) , hydrolysis , stereochemistry , protein folding , substitution (logic) , enzyme , combinatorial chemistry , biochemistry , biology , materials science , ecology , electrical engineering , composite material , engineering , programming language , computer science
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. on page 712 in Issue 8, 2016 (DOI: 10.1002/cbic.201500312).