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Spectroscopic study on the interaction between mononaphthalimide spermidine (MINS) and bovine serum albumin (BSA)

Paper ID Volume ID Publish Year Pages File Format Full-Text
29788 44440 2015 7 PDF Available
Title
Spectroscopic study on the interaction between mononaphthalimide spermidine (MINS) and bovine serum albumin (BSA)
Abstract

•Polyamine-conjugate caused the conformational alteration of BSA.•MINS bound to BSA.•By and large, the fluorescent quenching mechanism was a static type.•The type of interaction force was mainly hydrophobic.•Docking model for compound 1 with BSA was also investigated.

The interaction mononaphthalimide spermidine (MINS, 1) and bovine serum albumin (BSA) was studied by UV/vis absorption, fluorescence and circular dichroism spectra (CD) under physiological conditions (pH = 7.4). The observed spectral quenching of BSA by compound 1 indicated compound 1 could bind to BSA. Further fluorescent tests revealed that the quenching mechanism of BSA by compound 1 was overall static. Meanwhile, the obtained binding constant and thermodynamic parameters on compound-BSA interaction showed that the type of interaction force of compound 1 and BSA was mainly hydrophobic. The analysis of synchronous, three-dimensional fluorescence and CD showed that compound 1 had weak influence on the conformational changes in BSA. Molecular docking simulation was performed and docking model in silico suggested that the configuration of compound 1 was localized in enzymatic drug site II in BSA. Furthermore, naphthalimide moiety of compound 1 greatly contributed to the hydrophobic interaction between compound 1 and BSA protein, as confirmed by experimental data.

Graphical abstractThe interaction between mononaphthalimide spermidine (MINS) with bovine serum albumin (BSA) was studied by UV/vis absorption, fluorescent and dichroism spectra (CD) under physiological conditions. Docking model for compound 1 with BSA was also investigated.Figure optionsDownload full-size imageDownload as PowerPoint slide

Keywords
Mononaphthalimide spermidine; Bovine serum albumin (BSA); Spectroscopic methods; Molecular docking
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Spectroscopic study on the interaction between mononaphthalimide spermidine (MINS) and bovine serum albumin (BSA)
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 142, January 2015, Pages 103–109
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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
Online Support
Any Questions? feel free to contact us