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Inhibition of Chymotrypsin by a Self‐Assembled DNA Quadruplex Functionalized with Cyclic Peptide Binding Fragments
Author(s) -
Cai Jianfeng,
Rosenzweig Brooke A.,
Hamilton Andrew D.
Publication year - 2009
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200801637
Subject(s) - chymotrypsin , peptide , dna , chemistry , scaffold , combinatorial chemistry , computational biology , biochemistry , stereochemistry , microbiology and biotechnology , enzyme , biology , computer science , database , trypsin
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 K i app =0.33 μ M . Detailed kinetic analysis revealed a two‐step slow binding inhibition mechanism for the inhibition of ChT by this inhibitor.