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Betulinic acid binding to human serum albumin: A study of protein conformation and binding affinity

Paper ID Volume ID Publish Year Pages File Format Full-Text
30899 44513 2009 5 PDF Available
Title
Betulinic acid binding to human serum albumin: A study of protein conformation and binding affinity
Abstract

Betulinic acid (BA) has anti cancer and anti-HIV activity and has been proved to be therapeutically effective against cancerous and HIV-infected cells. Human serum albumin (HSA) is the predominant protein in the blood. Most drugs that bind to HSA will be transported to other parts of the body. Using micro TOF-Q mass spectrometry, we have shown, for the first time that BA isolated from a plant (Tephrosia calophylla) binds to HSA. The binding constant of BA to HSA was calculated from fluorescence data and found to be KBA = 1.685 ± 0.01 × 106 M−1, indicating a strong binding affinity. The secondary structure of the HSA–BA complex was determined by circular dichroism. The results indicate that the HSA in this complex is partially unfolded. Further, binding of BA at nanomolar concentrations of BA to free HSA was detected using micro TOF-Q mass spectrometry. The study revealed a mass increase from 65199 Da (free HSA) to 65643 Da (HSA + drug), where the additional mass of 444 Da was due to bound BA. Based on the results of this study, it is suggested that micro TOF-Q mass spectrometry is useful technique for drug binding studies.

Keywords
Betulinic acid; Binding constants; Circular dichroism; Human serum albumin; Micro TOF-Q mass spectrometry; Tephrosia calophylla
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Betulinic acid binding to human serum albumin: A study of protein conformation and binding affinity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 94, Issue 1, 9 January 2009, Pages 8–12
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
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Full-text PDF Download
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