Interaction of the anticancer plant alkaloid sanguinarine with bovine serum albumin.

ABSTRACT:

Background

Interaction of the iminium and alkanolamine forms of sanguinarine with bovine serum albumin (BSA) was characterized by spectroscopic and calorimetric techniques.

Methodology/principal findings

Formation of strong complexes of BSA with both iminium and alkanolamine forms was revealed from fluorescence quenching of sanguinarine. Binding parameters calculated from Stern-Volmer quenching method revealed that the neutral alkanolamine had higher affinity to BSA compared to the charged iminium form. Specific binding distances of 3.37 and 2.38 nm between Trp 212 (donor) and iminium and alkanolamine forms (acceptor), respectively, were obtained from Forster resonance energy transfer studies. Competitive binding using the site markers warfarin and ibuprofen, having definite

SUBMITTER: Hossain M 

PROVIDER: S-EPMC3071820 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature