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Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.

Abstract:

The efficient binding and inhibition of α-chymotrypsin (ChT) by a self-assembled DNA quadruplex with protein recognition fragments appended on the 5'-ends of the assembled G-quartet was reported. The peptide loops were constructed such that they are broadly complementary to the cationic and hydrophobic active site region of ChT. The single-strand peptide loop adduct presents only a single monomeric peptide loop to the protein and displays the weakest inhibition. The factorial velocities for t...

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Publication status:
Published

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Publisher copy:
10.1002/chem.200801637

Authors


Rosenzweig, BA More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Journal:
Chemistry (Weinheim an der Bergstrasse, Germany)
Volume:
15
Issue:
2
Pages:
328-332
Publication date:
2009
DOI:
EISSN:
1521-3765
ISSN:
0947-6539
URN:
uuid:2181de28-eef3-4c80-a9cf-20ff1079636f
Source identifiers:
117470
Local pid:
pubs:117470

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