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Cover Picture: The Design and Evaluation of Heparin‐Binding Foldamers (Angew. Chem. Int. Ed. 41/2005)
Author(s) -
Choi Sungwook,
Clements Dylan J.,
Pophristic Vojislava,
Ivanov Ivaylo,
Vemparala Satyavani,
Bennett Joel S.,
Klein Michael L.,
Winkler Jeffrey D.,
DeGrado William F.
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200590137
Subject(s) - antithrombin , heparin , chemistry , amide , int , cover (algebra) , sequence (biology) , stereochemistry , low molecular weight heparin , biochemistry , computer science , engineering , mechanical engineering , operating system
Small inhibitors for low‐molecular‐weight heparin, namely short aryl amide foldamers, were designed with the aid of molecular‐dynamics calculations. The cover picture shows that the binding is primarily dominated by electrostatic interactions between a pentasaccharide sequence of heparin and the antagonist. In their Communication on page 6685 ff., W. F. DeGrado and co‐workers show that heparin binds and modulates the biological properties of a number of proteins, including antithrombin II and factor Xa.