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...
Príomhchruthaitheoirí: | , , |
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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. |
first_indexed | 2024-03-06T19:43:38Z |
format | Journal article |
id | oxford-uuid:2181de28-eef3-4c80-a9cf-20ff1079636f |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T19:43:38Z |
publishDate | 2009 |
record_format | dspace |
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 |