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Cover Picture: Bicyclic Peptides with Optimized Ring Size Inhibit Human Plasma Kallikrein and its Orthologues While Sparing Paralogous Proteases (ChemMedChem 7/2012)
Author(s) -
Baeriswyl Vanessa,
Rapley Helen,
Pollaro Lisa,
Stace Catherine,
Teufel Dan,
Walker Edward,
Chen Shiyu,
Winter Greg,
Tite John,
Heinis Christian
Publication year - 2012
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201290029
Subject(s) - proteases , kallikrein , bicyclic molecule , peptide , serine , serine protease , phage display , chemistry , potency , ring size , cover (algebra) , human plasma , protease , biochemistry , stereochemistry , ring (chemistry) , biology , computational biology , in vitro , enzyme , chromatography , organic chemistry , mechanical engineering , engineering
The cover picture shows a novel bicyclic peptide inhibitor of the serine protease plasma kallikrein identified by phage display. By modulating the loop size of the peptide macrocycles, inhibitors with sub‐nanomolar potency and an optimal specificity profile could be generated. For more details, see the Communication by Greg Winter, John Tite, Christian Heinis et al. on p. 1173 ff.