当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Spectroscopic analysis of the interaction of valproic acid with histone H1 in solution and in chromatin structure.

Spectroscopic analysis of the interaction of valproic acid with histone H1 in solution and in chromatin structure.

Abstract：

:Histone H1 is a basic chromosomal protein which links adjacent nucleosomes in chromatin structure. Valproic acid (VPA), a histone deacetylase inhibitor, is widely used as an antiepileptic drug for the treatment of various cancers. In this study the interaction between VPA and histone H1, chromatin and DNA in solution was investigated employing spectroscopic techniques. The results showed that VPA binds cooperatively to histone H1 and chromatin but exhibited very weak interaction with DNA. The association constants demonstrated higher affinity of VPA to H1 compared to chromatin. Fluorescence emission intensity was reduced by quenching value (Ksv) of 2.3 and 0.83 for H1 and chromatin respectively. VPA also altered ellipticity of chromatin and H1 at 220nm indicating increase in α-helix content of H1/chromatin proteins suggesting that the protein moiety of chromatin is the site of VPA action. Moreover, thermal denaturation revealed hypochromicity in chromatin Tm profiles with small shift in Tm values without any significant change in DNA pattern. It is concluded that VPA, apart from histone deacetylase inhibition activity, binds strongly to histone H1 in chromatin structure, demonstrating that VPA may also exert its anticancer activity by influencing chromatin proteins which opens new insight into the mechanism of VPA action.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Sargolzaei J,Rabbani-Chadegani A,Mollaei H,Deezagi A

doi

10.1016/j.ijbiomac.2017.02.098

subject

Has Abstract

pub_date

2017-06-01 00:00:00

pages

427-432

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(17)30291-X

journal_volume

99

pub_type

杂志文章

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