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Journal of Biochemistry Advance Access originally published online on December 15, 2006
Journal of Biochemistry 2007 141(2):261-268; 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 Gull1, Priyankar Sen2, Kabir-ud-Din1 and Rizwan Hasan Khan2,*

1Department of Chemistry; and 2Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh–202002, India

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

Received November 20, 2006; Accepted December 10, 2006


  Abstract

We report that the presence of very low concentrations (<0.1 M) 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 10 mM urea (U) and 20 mM 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: ANS binding and human serum albumin, circular dichroism, intrinsic fluorescence, monomethyl urea, urea

Abbreviations: ANS, 1-anilino-8-naphthalenesulphonicacid; CD, circular dichroism; HSA, human serum albumin; MMU, monomethyl urea; U, urea


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