Structural changes of human serum albumin in response to a low concentration of heavy ions.
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.
Saha
Anushree
A
Department of Physics, University of Wisconsin-Milwaukee, P.O. Box 413, Milwaukee, WI 53201, USA. asaha@uwm.edu
Yakovlev
Vladislav V
VV
D000042:Absorption; D004305:Dose-Response Relationship, Drug; D020450:Heavy Ions; D006801:Humans; D007854:Lead / Q000494:pharmacology*; D008958:Models, Molecular; D055620:Optical Phenomena; D055503:Protein Multimerization / Q000187:drug effects; D020836:Protein Structure, Quaternary / Q000187:drug effects; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D012996:Solutions; D013057:Spectrum Analysis
D012709:Serum Albumin; D012996:Solutions; D007854:Lead