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

Jianfeng Cai, Brooke A. Rosenzweig, Andrew D. Hamilton

Research output: Contribution to journalArticlepeer-review

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 the hydrolysis of N-benzoyl tyrosine p-nitroanilide by ChT as a function of preincubation time for different concentrations show a two-step mechanism of inhibition. The protein fragment is also found to display the highest inhibition potency for ChT and also found to be a good inhibitor.

Original languageEnglish (US)
Pages (from-to)328-332
Number of pages5
JournalChemistry - A European Journal
Volume15
Issue number2
DOIs
StatePublished - Jan 2 2009

Keywords

  • Chymotrypsin
  • DNA structures
  • Incubation
  • Inhibition
  • Receptors

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry

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