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Activation Of P300 Histone Acetyltransferase By Small Molecules Altering Enzyme Structure: Period Probed By Surface Enhanced Raman Spectroscopy

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dc.contributor.author Mantelingu, K
dc.contributor.author Kishore, A Hari
dc.contributor.author Balasubramanyam, K
dc.contributor.author Kumar, G V Pavan
dc.contributor.author Altaf, M
dc.contributor.author Swamy, S Nanjunda
dc.contributor.author Selvi, Ruthrotha
dc.contributor.author Das, Chandrima
dc.contributor.author Narayana, Chandrabhas
dc.contributor.author Rangappa, K S
dc.contributor.author Kundu, Tapas K
dc.date.accessioned 2012-02-20T10:34:34Z
dc.date.available 2012-02-20T10:34:34Z
dc.date.issued 2007-05-03
dc.identifier 1520-6106 en_US
dc.identifier.citation Journal of Physical Chemistry B 111(17), 4527-4534 (2007) en_US
dc.identifier.uri https://libjncir.jncasr.ac.in/xmlui/10572/475
dc.description Restricted Access en_US
dc.description.abstract Reversible acetylation of nucleosomal histones and nonhistone proteins play pivotal roles in the regulation of all the DNA templated phenomenon. Dysfunction of the enzymes involved in the acetylation/deacetylation leads to several diseases. Therefore, these enzymes are the targets for new generation therapeutics. Here, we report the synthesis of trifluoromethyl phenyl benzamides and their effect on histone acetyltransferase (HAT) activity of p300. One of these benzamides, CTPB (N-(4-chloro-3-trifluoromethyl-phenyl)-2-ethoxy-6-pentadecyl-benzamide), was discovered as a potent activator of the p300 HAT activity. We have found that pentadecyl hydrocarbon chain of CTPB is required to activate the HAT only under certain context. Furthermore, our results show that the relative position of −CF3 and −Cl in CTB (N-(4-chloro-3-trifluoromethyl-phenyl)-2-ethoxy-benzamide) is also very critical for the activation. Surface-enhanced Raman spectroscopy (SERS) of p300 and the HAT activator complexes evidently suggest that the activation of HAT activity is achieved by the alteration of p300 structure. Therefore, apart from elucidating the chemical basis for small molecule mediated activation of p300, this report also describes, for the first time, Raman spectroscopic analysis of the complexes of histone-modifying enzymes and their modulators, which may be highly useful for therapeutic applications. en_US
dc.description.uri http://dx.doi.org/10.1021/jp067655s en_US
dc.language.iso en en_US
dc.publisher American Chemical Society en_US
dc.rights © 2007 American Chemical Society en_US
dc.subject Anacardic Acids-chemistry en_US
dc.subject Benzamides-chemistry en_US
dc.subject Benzamides-pharmacology en_US
dc.subject Cell Cycle Proteins-chemistry en_US
dc.subject Cell Cycle Proteins-metabolism en_US
dc.subject Enzyme Activation-drug effects en_US
dc.subject HeLa Cells en_US
dc.subject Histone Acetyltransferases-chemistry en_US
dc.subject Histone Acetyltransferases-metabolism en_US
dc.subject Humans en_US
dc.subject Hydrocarbons-chemistry en_US
dc.subject Kinetics en_US
dc.subject Molecular Structure en_US
dc.subject Salicylic Acid-chemistry en_US
dc.subject Spectrum Analysis en_US
dc.subject Raman en_US
dc.subject Transcription Factors-chemistry en_US
dc.subject Transcription Factors-metabolism en_US
dc.subject p300-CBP Transcription Factors en_US
dc.title Activation Of P300 Histone Acetyltransferase By Small Molecules Altering Enzyme Structure: Period Probed By Surface Enhanced Raman Spectroscopy en_US
dc.type Article en_US


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