The thermal analysis of nonezymatic glycosylation of human serum albumin: differential scanning calorimetry and circular dichroism studies

The thermal analysis of nonezymatic glycosylation of human serum albumin: differential scanning calorimetry and circular dichroism studies

The stability of human serum albumin (HSA) is studied before and after incubation with glucose utilizing differential scanning Calorimetry (DSC) and circular dichroism (CD) techniques. The incubation of HSA with glucose results in its nonenzymatic glycosylation that is glycosylated HSA (GHSA) formed...

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Bibliographic Details
Published in:Thermochimica acta Vol. 389; no. 1; pp. 141 - 151
Main Authors: Mohamadi-Nejad, A., Moosavi-Movahedi, A.A., Safarian, S., Naderi-Manesh, M.H., Ranjbar, B., Farzami, B., Mostafavi, H., Larijani, M.B., Hakimelahi, G.H.
Format: Journal Article
Language:English
Published: Amsterdam Elsevier B.V 01-07-2002
Elsevier Science
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
DSC
Fundamental and applied biological sciences. Psychology
Glycosylation
HSA
Miscellaneous
Proteins
Thermal analysis
CD
Glycosylation
Thermal analysis
DSC
HSA
Human
Differential scanning calorimetry
Circular dichroism spectrum
Stability
Albumin
Helical structure
Serum albumin
Serum protein
Secondary structure
Conformation
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Summary:The stability of human serum albumin (HSA) is studied before and after incubation with glucose utilizing differential scanning Calorimetry (DSC) and circular dichroism (CD) techniques. The incubation of HSA with glucose results in its nonenzymatic glycosylation that is glycosylated HSA (GHSA) formed in glucose concentrations (8.25, 16.5 and 27.5 mM) in a temperature dependent manner. The DSC profiles of GHSA samples, which indicate changes in heat capacity C p and C p excess versus temperature, were obtained and the thermal denaturation reversibility of each sample was assessed up to 80 °C. The melting point ( T m), the change of enthalpy, and the heat capacity for GHSA at different glucose concentrations were obtained. The results showed that glucose at lower concentrations induces the destabilization of HSA while at higher concentrations induces its stabilization. In addition, considerable conformational changes in HSA were observed after incubation with glucose. This was demonstrated through deconvolution of DSC profiles that imply the formation of new energetic domains, which were further confirmed by the presence of α-helices in the CD spectrum.
ISSN:0040-6031
1872-762X
DOI:10.1016/S0040-6031(02)00006-0