Literature DB >> 26139532

A Spectroscopy Approach for the Study of the Interaction of Oxovanadium(IV)-Salen Complexes with Proteins.

Alagarsamy Mathavan1, Arumugam Ramdass, Seenivasan Rajagopal.   

Abstract

Oxovanadium(IV)-salen complexes bind with bovine serum albumin (BSA) and ovalbumin (OVA) strongly with binding constant in the range 10(4)-10(7) M(-1) at physiological pH (7.4) confirmed using UV-visible absorption, fluorescence spectral and circular dichroism (CD) study. CD results show that the binding of oxovanadium(IV) complexes induces the conformational change with the loss of α-helicity in the proteins. Docking studies indicate that mode of binding of oxovanadium(IV)-salen complexes with proteins is hydrophobic in nature.

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Year:  2015        PMID： 26139532     DOI： 10.1007/s10895-015-1604-3

Source DB:  PubMed          Journal:  J Fluoresc        ISSN： 1053-0509            Impact factor:   2.217


  43 in total

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Journal:  J Am Chem Soc       Date:  2005-04-13       Impact factor: 15.419

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Authors:  Yi Zhang; Dean E Wilcox
Journal:  J Biol Inorg Chem       Date:  2001-11-01       Impact factor: 3.358

Review 9.  Ficoll and dextran vs. globular proteins as probes for testing glomerular permselectivity: effects of molecular size, shape, charge, and deformability.

Authors:  Daniele Venturoli; Bengt Rippe
Journal:  Am J Physiol Renal Physiol       Date:  2005-04

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Authors:  W Bal; J Christodoulou; P J Sadler; A Tucker
Journal:  J Inorg Biochem       Date:  1998-04       Impact factor: 4.155
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  1 in total

1.  Comparative Study of the Interactions between Ovalbumin and five Antioxidants by Spectroscopic Methods.

Authors:  Xiangrong Li; Yunhui Yan
Journal:  J Fluoresc       Date:  2016-10-08       Impact factor: 2.217
  1 in total

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