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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Consequential alterations in haemoglobin structure upon glycation with fructose: prevention by acetylsalicylic acid
M Bakhti1, M Habibi-Rezaei, A A Moosavi-Movahedi
1School of Biology, University College of Science, University of Tehran; Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Abstract:
Increased fructose concentration in erythrocytes of diabetic patients subject haemoglobin (Hb) to be glycated by fructose. Haemoglobin glycation results in early and advanced glycation end products which are known as HbA(1c) and Hb-AGE, respectively. In diabetics the Hb-AGE content raises and the mean parameter multiplication value (PMV) for Hb-AGE has been calculated at 6 against non-diabetics. We are emphasizing on fluorescence descriptive pairs especially of 370/440 nm (lambda(ex)/lambda(em)) and thioflavin T binding process to characterize short-term Hb-AGE formation upon glycation with fructose or fructation. Secondary structure elements were estimated after far-UV circular dichroism spectropolarimetery which reveals up to 11.3% beta-content attainment for 20 days incubated Hb with fructose which is concurred with enhanced hydrophobicity of the protein. The later is described through enhanced 1-anilino-8-naphthalene sulphonate (ANS) binding to fructated protein. The preventive effect of acetylsalicylic acid on glycation of methemoglobin and consequently, Hb-AGE formation also has been included.
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