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

Jianfeng Cai, Brooke A. Rosenzweig, Andrew Hamilton

Research output: Contribution to journalArticle

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

Fingerprint

Cyclic Peptides
Chymotrypsin
Peptides
DNA
Proteins
Hydrolysis
Tyrosine

Keywords

  • Chymotrypsin
  • DNA structures
  • Incubation
  • Inhibition
  • Receptors

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments. / Cai, Jianfeng; Rosenzweig, Brooke A.; Hamilton, Andrew.

In: Chemistry - A European Journal, Vol. 15, No. 2, 02.01.2009, p. 328-332.

Research output: Contribution to journalArticle

@article{0192cfb1cfce442bb34ecdfbf5d5f36a,
title = "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 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.",
keywords = "Chymotrypsin, DNA structures, Incubation, Inhibition, Receptors",
author = "Jianfeng Cai and Rosenzweig, {Brooke A.} and Andrew Hamilton",
year = "2009",
month = "1",
day = "2",
doi = "10.1002/chem.200801637",
language = "English (US)",
volume = "15",
pages = "328--332",
journal = "Chemistry - A European Journal",
issn = "0947-6539",
publisher = "Wiley-VCH Verlag",
number = "2",

}

TY - JOUR

T1 - Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments

AU - Cai, Jianfeng

AU - Rosenzweig, Brooke A.

AU - Hamilton, Andrew

PY - 2009/1/2

Y1 - 2009/1/2

N2 - 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.

AB - 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.

KW - Chymotrypsin

KW - DNA structures

KW - Incubation

KW - Inhibition

KW - Receptors

UR - http://www.scopus.com/inward/record.url?scp=58449085187&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=58449085187&partnerID=8YFLogxK

U2 - 10.1002/chem.200801637

DO - 10.1002/chem.200801637

M3 - Article

VL - 15

SP - 328

EP - 332

JO - Chemistry - A European Journal

JF - Chemistry - A European Journal

SN - 0947-6539

IS - 2

ER -