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Determination of Allosteric Effects and Interstrand Bidentate Interactions in DNA‐Peptide Molecular Recognition
Author(s) -
Chen YenChung,
Huang Jonathan T. B.,
Jeng KeeChing G.,
Yang Robin C. K.,
Liao MoKai,
Chen CheeShan,
Chien WeiJyun,
Wey MingTsair,
Kan LouSing,
Sheh Leung
Publication year - 2010
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201000041
Subject(s) - chemistry , dna , peptide , cooperativity , allosteric regulation , circular dichroism , footprinting , oligonucleotide , stereochemistry , biochemistry , biophysics , enzyme , base sequence , biology
To study DNA allostery, quantitative DNase I footprinting studies were carried out on a newly designed peptide His‐Hyp‐Lys‐Lys‐(Py) 4 ‐Lys‐Lys‐NH 2 (HypKK‐10) containing the XHypKK (Hyp = hydroxyproline) and polyamide motifs. The interconnection of DNA footprints of peptides HypKK‐10 and the parent peptide PyPro‐12 supports the proposal that interaction network cooperativity is preferred in DNA‐peptide interactions between multiple recognition sites. A simple method of determining interstrand bidentate interactions between the peptide moieties and DNA bases is introduced. It is envisaged that interstrand bidentate interactions also participate in the relay of conformational changes to recognition sites on the complementary strands. Circular dichroism studies of the titration of peptide HypKK‐10 with an oligonucleotide duplex indicate that this peptide binds in a dimeric fashion to DNA in the minor groove. This work may prompt the design of new DNA binding ligands for the study of DNA‐peptide allosteric interactions and DNA interaction network.