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Inside Back Cover: Inhibition of Kallikrein‐Related Peptidases 7 and 5 by Grafting Serpin Reactive‐Center Loop Sequences onto Sunflower Trypsin Inhibitor‐1 (SFTI‐1) (ChemBioChem 8/2016)
Author(s) -
Jendrny Cathleen,
BeckSickinger Annette G.
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.201600146
Subject(s) - serpin , kallikrein , proteases , trypsin , peptide , serine protease , chemistry , cyclic peptide , biochemistry , protease , rational design , protease inhibitor (pharmacology) , serine , ramachandran plot , biology , protein structure , enzyme , genetics , gene , virus , antiretroviral therapy , viral load
The inside back cover picture shows a rational peptide‐design approach for the development of inhibitors of the serine proteases kallikrein‐related peptidases 7 (KLK7) and 5 (KLK5). Hybrid peptides combining the scaffold of the bicyclic peptide sunflower trypsin inhibitor‐1 (SFTI‐1) with amino acid sequences derived from the reactive center loops of different serpins were generated by solid‐phase peptide synthesis. Some of these molecules displayed nanomolar protease inhibition, and it was demonstrated that selectivity towards KLK5 and KLK7 could be transferred from the irreversible protease inhibitors of the serpin family to reversible canonical inhibitors. (Design: Stefanie Wittrisch) More information can be found in the full paper by A. G. Beck‐Sickinger and C. Jendrny on page 719 in Issue 8, 2016 (DOI: 10.1002/cbic.201500539).