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

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 hyd...

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Príomhchruthaitheoirí: Cai, J, Rosenzweig, B, Hamilton, A
Formáid: Journal article
Teanga:English
Foilsithe / Cruthaithe: 2009
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author Cai, J
Rosenzweig, B
Hamilton, A
author_facet Cai, J
Rosenzweig, B
Hamilton, A
author_sort Cai, J
collection OXFORD
description 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.
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spelling oxford-uuid:2181de28-eef3-4c80-a9cf-20ff1079636f2022-03-26T11:33:53ZInhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2181de28-eef3-4c80-a9cf-20ff1079636fEnglishSymplectic Elements at Oxford2009Cai, JRosenzweig, BHamilton, AThe 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.
spellingShingle Cai, J
Rosenzweig, B
Hamilton, A
Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.
title Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.
title_full Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.
title_fullStr Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.
title_full_unstemmed Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.
title_short Inhibition of chymotrypsin by a self-assembled DNA quadruplex functionalized with cyclic peptide binding fragments.
title_sort inhibition of chymotrypsin by a self assembled dna quadruplex functionalized with cyclic peptide binding fragments
work_keys_str_mv AT caij inhibitionofchymotrypsinbyaselfassembleddnaquadruplexfunctionalizedwithcyclicpeptidebindingfragments
AT rosenzweigb inhibitionofchymotrypsinbyaselfassembleddnaquadruplexfunctionalizedwithcyclicpeptidebindingfragments
AT hamiltona inhibitionofchymotrypsinbyaselfassembleddnaquadruplexfunctionalizedwithcyclicpeptidebindingfragments