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Journal of Biochemistry Advance Access published online on December 15, 2006
Journal of Biochemistry, doi:10.1093/jb/mvm027
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© 2006 The Japanese Biochemical Society

Effect of Physiological Concentration of Urea on The Conformation of Human Serum Albumin

Nuzhat Gulla, Priyankar Senb, Kabir-ud-Dina and Rizwan Hasan Khanb,*

a Department of Chemistry, Aligarh Muslim University, Aligarh – 202 002, India.
b Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh – 202002, India.

* To whom correspondence should be addressed. Rizwan Hasan Khan. Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh – 202002, India. E-mail: rizwanhkhan{at}hotmail.com, rizwanhkhan1{at}yahoo.com, Phone: 91-571-2720388, Fax: + 91-571-2721776

Received November 20, 2006; Accepted December 10, 2006


  Abstract

We report that the presence of very low concentrations (<0.1M) of urea, a widely used chemical denaturant, induces structure formation in the water-soluble globular protein human serum albumin (HSA) at pH 7. We have presented results suggesting an almost 8% and 5% increase in {alpha}-helix in the presence of 10mM urea (U) and 20mM monomethylurea (MMU) respectively. Far and near-UV circular dichroism studies along with tryptophan fluorescence and 1-anilino-8-naphthalenesulphonicacid (ANS) binding support our view. We hypothesize that both U and MMU, at such low concentrations, modify the solvent structure, increase the dielectric constant and consequently increase hydrophobic forces resulting in enhanced {alpha}-helical content. The implications of these results of the lower urea regime are significant because the physiological blood urea ranges from 2.5 to 7.5 mM.

Key Words: urea, mono-methyl urea, circular dichroism, intrinsic fluorescence, ANS binding and Human Serum Albumin


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