Inhibition of Chymotrypsin by a Self‐Assembled DNA Quadruplex Functionalized with Cyclic Peptide Binding Fragments

Abstract

A novel family of synthetic receptors was prepared for protein-surface recognition. The inhibition of chymotrypsin was achieved through protein-surface binding by four peptide loops arrayed on a DNA quadruplex scaffold (see figure). The most potent identified inhibitor has a Kiapp=0.33 μM. Detailed kinetic analysis revealed a two-step slow binding inhibition mechanism for the inhibition of ChT by this inhibitor. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.