Structural changes of human serum albumin in response to a low concentration of heavy ions. Academic Article

abstract

• Lead ions in solution interact strongly with human serum albumin and modify the properties and function of albumin molecules. In the present study, we used optical spectroscopic techniques to explore the binding sites of lead, present in albumin. Structural and chemical analysis of albumin molecules using fluorescence and Raman spectroscopy, predicted the modification of two major amino acids in albumin due to lead binding. No secondary structural changes are observed in the protein molecule, which is further confirmed using circular dichroism absorption measurements. The results indicate that loss of charge from the binding site of albumin by the charged lead ions, give rise to dipole interaction which acts as the major contributor to promote protein agglomeration.

authors

• Yakovlev, Vladislav

published proceedings

• J Biophotonics

author list (cited authors)

• Saha, A., & Yakovlev, V. V.

citation count

• 25

complete list of authors

• Saha, Anushree||Yakovlev, Vladislav V

publication date

• October 2010

publisher

• Wiley  Publisher

published in

• Journal of Biophotonics  Journal

keywords

• Absorption
• Dose-Response Relationship, Drug
• Heavy Ions
• Humans
• Lead
• Models, Molecular
• Optical Phenomena
• Protein Multimerization
• Protein Structure, Quaternary
• Serum Albumin
• Solutions
• Spectrum Analysis

PubMed Central ID

• 20635428

Digital Object Identifier (DOI)

• 10.1002/jbio.201000044

start page

• 670

end page

• 677

volume

• 3

issue

• 10-11

URL

• http%3A%2F%2Fdx.doi.org%2F10.1002%2Fjbio.201000044