Abstract
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.
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