Repository of Research and Investigative Information

Repository of Research and Investigative Information

Ilam University of Medical Sciences

Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy

Thu Oct 6 08:04:14 2022

(2006) Conformational study of human serum albumin in pre-denaturation temperatures by differential scanning calorimetry, circular dichroism and UV spectroscopy. Journal of Biochemistry and Molecular Biology. pp. 530-536. ISSN 12258687 (ISSN)

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Official URL: https://www.scopus.com/inward/record.uri?eid=2-s2....

Abstract

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 25°C to 55°C 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. 42°C. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at 45°C and 35°C 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 45°C compared to 35°C, 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.

Item Type: Article
Creators:
CreatorsEmail
Rezaei-Tavirani, M.UNSPECIFIED
Moghaddamnia, S. H.UNSPECIFIED
Ranjbar, B.UNSPECIFIED
Amani, M.UNSPECIFIED
Marashi, S. A.UNSPECIFIED
Keywords: Circular dichroism Conformational changes Differential scanning microcalorimetry HSA Sodium dodecyl sulphate dodecyl sulfate sodium serum albumin article chemistry differential scanning calorimetry human protein binding protein conformation protein folding protein secondary structure temperature thermodynamics ultraviolet spectrophotometry Calorimetry, Differential Scanning Humans Protein Structure, Secondary Sodium Dodecyl Sulfate Spectrophotometry, Ultraviolet
Divisions:
Page Range: pp. 530-536
Journal or Publication Title: Journal of Biochemistry and Molecular Biology
Journal Index: Scopus
Volume: 39
Number: 5
ISSN: 12258687 (ISSN)
Depositing User: مهندس مهدی شریفی
URI: http://eprints.medilam.ac.ir/id/eprint/1685

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