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Structural Stability as a Probe for Molecular Evolution of Homologous Albumins Studied by Spectroscopy and Bioinformatics

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Abstract

Equilibrium unfolding by guanidinium hydrochloride (GuHCl) and urea as well as evolutionary trends of two homologous albumins, pig serum albumin (PSA) and rabbit serum albumin (RSA), has been studied with circular dichroism, tryptophanyl fluorescence and bioinformatics. GuHCl cannot distinguish the contribution of electrostatic interactions to the proteins which were otherwise effectively monitored by urea. Higher differences in free energy changes due to urea than GuHCl show electrostatic interactions among charged amino acids are possibly responsible for higher structural stability of RSA in comparison to PSA. From the sequence of HSA and RSA, deletion of arginine at position 117 and the presence of one extra tryptophan at position 135 may possess some clue for lesser stability of PSA. Here, for comparison, chemical unfolding data of HSA and BSA had been taken into consideration. We found that thermodynamically RSA and PSA are closer to HSA and BSA, respectively, in accordance with their sequence homologies. Taxonomically, rabbit belongs to lagomorph which is closer to hominids than ungulates. Hence, on the basis of these thermodynamic data of protein denaturation of different species we can use this new approach to analyze the phylogenetic relationship among the major clades of eutherian mammals to obtain their evolutionary trends.

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Abbreviations

BSA:

Bovine serum albumin

CD:

Circular dichroism

ΔC hydp :

Net heat capacity change of hydration

GuHCl:

Guanidinium hydrochloride

\( \Updelta G_{\text{u}}^{\text{w}} \) :

Change in unfolding free energy in the absence of denaturant

HSA:

Human serum albumin

MRE:

Mean residue ellipticity

PSA:

Porcine serum albumin

RSA:

Rabbit serum albumin

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Acknowledgments

E. Ahmad and P. Sen thank Council of Scientific and Industrial Research, and Department of Biotechnology, Govt. of India for financial assistance in the form of SRF.

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Authors and Affiliations

  1. Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, India

    Ejaz Ahmad, Priyankar Sen & Rizwan Hasan Khan

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  1. Ejaz Ahmad
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  2. Priyankar Sen
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  3. Rizwan Hasan Khan
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Correspondence to Rizwan Hasan Khan.

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Ejaz Ahmad and Priyankar Sen contributed equally to this study.

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Ahmad, E., Sen, P. & Khan, R.H. Structural Stability as a Probe for Molecular Evolution of Homologous Albumins Studied by Spectroscopy and Bioinformatics. Cell Biochem Biophys 61, 313–325 (2011). https://doi.org/10.1007/s12013-011-9214-4

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