Journal Title
Title of Journal: J Incl Phenom Macrocycl Chem
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Abbravation: Journal of Inclusion Phenomena and Macrocyclic Chemistry
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Publisher
Springer Netherlands
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Authors: Atanu Singha Roy Pooja Ghosh Swagata Dasgupta
Publish Date: 2016/05/06
Volume: 85, Issue: 3-4, Pages: 193-202
Abstract
Reducing sugars can modify protein structures in vivo via nonenzymatic methods were identified in different cases of diabetes and glycemia The synthesis and characterization of glycated analogue of human serum albumin HSA has been reported recently by our group Singha Roy et al in J Biomol Struct Dyn 2015 doi 101080/0739110220151094749 The current paper is focused on the interaction of −epigallocatechin gallate EGCG a major green tea component with the glycated HSA The interaction of EGCG with the glycated HSA has been carried out using steadystate fluorescence and circular dichroism experiments The quenching constants k q were found in the order of 1013 M−1 s−1 indicating the presence of static quenching mode in the interaction The binding constants of EGCG–HSA complex was found to be decreased from 763 × 104 Maiti et al in Proteins Struct Funct Bioinform 64355–362 2006 to 327 × 104 M−1 at 293 K after glycation of HSA The changes in entropy ∆S° of the interaction of EGCG has been altered from +1623 with native HSA to +3484 J/K mol with glycated HSA which may offer a stabilization in αhelix of the glycated HSA during binding EGCG has shown its affinity to the site 1 subdomain IIA of the glycated HSA Energy transfer parameters revealed the possibility of nonradiative energy transfer from donor Trp 214 to acceptor EGCGSDG gratefully acknowledges Department of Science and Technology Govt of India Grant No SR/SO/BB054/2007 for financial support ASR is thankful to Council of Scientific Industrial Research CSIR New Delhi India for senior research fellowship Authors are grateful to IIT Kharagpur for the experimental facilities
Keywords:
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