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A spectroscopy approach for the study of the interactions of bioactive vanadium species with bovine serum albumin.

Abstract：

:The interest in biological functions (benefits or toxics effects) of vanadium species has grown enormously in recent years. In this work, different spectroscopic methods were applied to study the effects of the interaction of vanadyl and vanadate species with bovine serum albumin (BSA), considered as the most abundant plasma protein. UV-Vis, Fourier transform infrared (FT-IR), and FT-Raman spectroscopies were used to investigate changes in secondary and tertiary structures of BSA induced by the binding of oxovanadium(IV) and vanadate(V) species (VO(2+) and VO3(-), respectively). Correlations between the metal ion binding mode, protein conformational transitions, and structural variations were established.

journal_name

Bioorg Med Chem

journal_title

Bioorganic & medicinal chemistry

authors

Ferrer EG,Bosch A,Yantorno O,Baran EJ

doi

10.1016/j.bmc.2008.01.060

subject

Has Abstract

pub_date

2008-04-01 00:00:00

pages

3878-86

issue

7

eissn

0968-0896

issn

1464-3391

pii

S0968-0896(08)00063-1

journal_volume

16

pub_type

杂志文章

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