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Inside Cover: Bicyclic Peptide Inhibitor of Urokinase‐Type Plasminogen Activator: Mode of Action (ChemBioChem 16/2013)
Author(s) -
Roodbeen Renée,
Paaske Berit,
Jiang Longguang,
Jensen Jan K.,
Christensen Anni,
Nielsen Jakob T.,
Huang Mingdong,
Mulder Frans A. A.,
Nielsen Niels Chr.,
Andreasen Peter A.,
Jensen Knud J.
Publication year - 2013
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.201390059
Subject(s) - bicyclic molecule , plasminogen activator , serine protease , peptide , urokinase , chemistry , stereochemistry , biochemistry , protease , combinatorial chemistry , biology , enzyme , genetics
The inside cover picture shows the binding of a rationally designed bicyclic peptide inhibitor to the serine protease urokinase‐type plasminogen activator (uPA). On p. 2179 ff., K. J. Jensen et al. describe how a monocyclic peptide was transformed into a bicyclic peptide without loss of inhibitory properties but, rewardingly, with a reduced loss of entropy upon binding.