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Rezaei Tavirani, M et al.

Rezaei Tavirani, Moghaddamnia, Ranjbar, Amani, Marashi,

Conformational Study of Human Serum Albumin in Pre-denaturation Temperatures by Differential Scanning Calorimetry, Circular Dichroism and UV Spectroscopy.

Thermal conformational changes of human serum albumin (HSA) in phosphate buffer, 10 mM at pH = 7 are investigated using differential scanning calorimetric (DSC), circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature increment from 25oC to 55oC induces reversible conformational changes in the structure of HSA. Conformational change of HSA are shown to be a three-step process. Interestingly, melting temperature of the last domain is equal to the maximum value of fever in pathological conditions, i.e. 42oC. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at 45oC and 35oC reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA. Since HSA has a more affinity for SDS at 45oC compared to 35oC, It is suggested that the net negative charge of HSA is decreased in fever, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.[1]

References

Conformational Study of Human Serum Albumin in Pre-denaturation Temperatures by Differential Scanning Calorimetry, Circular Dichroism and UV Spectroscopy. Tavirani, M.R., Moghaddamnia, S.H., Ranjbar, B., Amani, M., Marashi, S.A. J. Biochem. Mol. Biol. (2006) [Pubmed]

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