Structural Alterations of Human Serum Albumin Caused by Glycative and Oxidative Stressors Revealed by Circular Dichroism Analysis

International Journal of Molecular Sciences

Fiammetta Monacelli³  Daniela Storace³  Cristina D𠆚rrigo¹  Roberta Sanguineti³  Roberta Borghi³  Davide Pacini³  Anna L. Furfaro²  Maria A. Pronzato²  Patrizio Odetti³ 

[1] Institute for Macromolecular Studies-ISMAC, National Research Council-CNR, Genova 16149, Italy; E-Mail:;Department of Experimental Medicine, Section of General Pathology, University of Genova, Genova 16132, Italy; E-Mails:;Department of Internal Medicine, University of Genova, Genova 16132, Italy; E-Mails:

关键词: ribose;    ascorbic acid;    pentosidine;    fluorescence;    circular dichroism;   

DOI  :  10.3390/ijms140610694

来源: mdpi

【 摘 要 】

The aim of this work was to evaluate the ability of oxidative and glycative stressors to modify properties of human serum albumin (HSA) by analyzing markers of glycation (pentosidine) and oxidation (advanced oxidative protein products (AOPPs)) and assessing fluorescence and circular dichroism. HSA was incubated for up to 21 days with ribose, ascorbic acid (AA) and diethylenetriamine pentacetate (DTPA) in various combinations in order to evaluate influences of these substances on the structure of HSA. Ribose was included as a strong glycative molecule, AA as a modulator of oxidative stress, and DTPA as an inhibitor of metal-catalyzed oxidation. Ribose induced a significant increase in pentosidine levels. AA and DTPA prevented the accumulation of pentosidine, especially at later time points. Ribose induced a mild increase in AOPP formation, while AA was a strong inducer of AOPP formation. Ribose, in combination with AA, further increased the formation of AOPP. DTPA prevented the AA-induced generation of AOPP. Ribose was also a potent inducer of fluorescence at 335nm ex/385nm em, which is typical of pentosidine. AA and DTPA prevented this fluorescence. Circular dichroism showed complex results, in which AA and DTPA were strong modifiers of the percentages of the alpha-helical structure of HSA, while ribose affected the structure of HSA only at later time points.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland