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Binding of a new bisphenol analogue, bisphenol S to bovine serum albumin and calf thymus DNA

Paper ID Volume ID Publish Year Pages File Format Full-Text
30297 44468 2014 9 PDF Available
Title
Binding of a new bisphenol analogue, bisphenol S to bovine serum albumin and calf thymus DNA
Abstract

•BPS binds to DNA by groove mode.•The binding site of BPS to BSA located in the subdomain IB.•The H-bonds and hydrophobic interactions played major roles in stabilizing the BPS–BSA/DNA complex.•The molecular docking study of BPS with BSA and DNA also supports the experimental results.

Interactions of bisphenol S, a new bisphenol analogue with bovine serum albumin and calf thymus DNA were investigated using different spectroscopic methods and molecular modeling calculation. According to the analysis of experimental and theoretical data, we concluded that hydrophobic interactions and hydrogen bonding primarily mediated the binding processes of bisphenol S with bovine serum albumin and DNA. In addition, the electrostatic force should not be excluded. Molecular modeling studies indicated that the binding site of bisphenol S to bovine serum albumin located in the subdomain IB, while bisphenol S was a groove binder of DNA. In addition, BPS did not obviously induce second structural changes of bovine serum albumin, but it induced a conformational change of calf thymus DNA.

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Keywords
Bisphenol S; DNA; Bovine serum albumin; Binding mode; Molecular modeling
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Binding of a new bisphenol analogue, bisphenol S to bovine serum albumin and calf thymus DNA
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 138, 5 September 2014, Pages 182–190
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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