Structural Alterations of Human Serum Albumin Caused by Glycative and Oxidative Stressors Revealed by Circular Dichroism Analysis
Autor: | Daniela Storace, Roberta Borghi, Roberta Sanguineti, Anna L. Furfaro, Patrizio Odetti, Fiammetta Monacelli, Cristina D'Arrigo, Maria Adelaide Pronzato, Nicola Traverso, Davide Pacini |
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Rok vydání: | 2013 |
Předmět: |
ribose
ascorbic acid pentosidine fluorescence circular dichroism Circular dichroism Glycosylation Serum albumin Acetates Arginine medicine.disease_cause Protein Structure Secondary Article Catalysis lcsh:Chemistry Inorganic Chemistry chemistry.chemical_compound Glycation Ribose medicine Humans Physical and Theoretical Chemistry Pentosidine lcsh:QH301-705.5 Molecular Biology Serum Albumin Spectroscopy biology Chemistry Lysine Organic Chemistry General Medicine Ascorbic acid Human serum albumin Computer Science Applications Oxidative Stress lcsh:Biology (General) lcsh:QD1-999 Biochemistry biology.protein Oxidation-Reduction Oxidative stress medicine.drug |
Zdroj: | International journal of molecular sciences (Online) 14 (2013): 10694–10709. doi:10.3390/ijms140610694 info:cnr-pdr/source/autori:Monacelli F.; Storace D.; D'Arrigo C.; Sanguineti R.; Borghi R.; Pacini D.; Furfaro A.L.; Pronzato M.A.; Odetti P.; Traverso N./titolo:Structural Alterations of Human Serum Albumin Caused by Glycative and Oxidative Stressors Revealed by Circular Dichroism Analysis/doi:10.3390%2Fijms140610694/rivista:International journal of molecular sciences (Online)/anno:2013/pagina_da:10694/pagina_a:10709/intervallo_pagine:10694–10709/volume:14 International Journal of Molecular Sciences; Volume 14; Issue 6; Pages: 10694-10709 International Journal of Molecular Sciences, Vol 14, Iss 6, Pp 10694-10709 (2013) International Journal of Molecular Sciences |
ISSN: | 1422-0067 |
DOI: | 10.3390/ijms140610694 |
Popis: | 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. |
Databáze: | OpenAIRE |
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