Spectroscopic Studies on the Molecular Ageing of Serum Albumin
Autor: | Bartosz Pawełczak, Anna Sułkowska, M. Maciążek-Jurczyk, Mariola Chudzik |
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Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
030103 biophysics Circular dichroism Aging molecular ageing serum albumin metoprolol second derivative circular dichroism Serum albumin Pharmaceutical Science Absorption (skin) Article Analytical Chemistry lcsh:QD241-441 03 medical and health sciences Residue (chemistry) lcsh:Organic chemistry Drug Discovery Animals Humans Computer Simulation Physical and Theoretical Chemistry skin and connective tissue diseases Binding Sites biology Chemistry Circular Dichroism Organic Chemistry Albumin Protein Structure Tertiary 030104 developmental biology Spectrometry Fluorescence Biochemistry Chemistry (miscellaneous) Ageing Toxicity biology.protein Molecular Medicine Cattle sense organs Isomerization Protein Binding |
Zdroj: | Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry Molecules; Volume 22; Issue 1; Pages: 34 Molecules, Vol 22, Iss 1, p 34 (2016) |
ISSN: | 1420-3049 |
Popis: | Pathological states in the organism, e.g., renal or hepatic diseases, cataract, dysfunction of coronary artery, diabetes mellitus, and also intensive workout, induce the structural modification of proteins called molecular ageing or N-A isomerization. The aim of this study was to analyze the structural changes of serum albumin caused by alkaline ageing using absorption, spectrofluorescence, and circular dichroism spectroscopy. The N-A isomerization generates significant changes in bovine (BSA) and human (HSA) serum albumin subdomains—the greatest changes were observed close to the tryptophanyl (Trp) and tyrosyl (Tyr) residue regions while a smaller change was observed in phenyloalanine (Phe) environment. Moreover, the changes in the polarity of the Trp neighborhood as well as the impact of the ageing process on α-helix, β-sheet content, and albumin molecule rotation degree have been analyzed. Based on the spectrofluorescence study, the alterations in metoprolol binding affinity to the specific sites that increase the toxicity of the drug were investigated. |
Databáze: | OpenAIRE |
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