Next Article in Journal
Fenofibrate Therapy Restores Antioxidant Protection and Improves Myocardial Insulin Resistance in a Rat Model of Metabolic Syndrome and Myocardial Ischemia: The Role of Angiotensin II
Next Article in Special Issue
Comparison of Hydrogels Based on Commercial Chitosan and Beetosan® Containing Nanosilver
Previous Article in Journal
Dysregulation of Cell Death and Its Epigenetic Mechanisms in Systemic Lupus Erythematosus
Previous Article in Special Issue
The Influence of Anionic Initiator on the Selected Properties of Poly-N-Isopropyl Acrylamide Evaluated for Controlled Drug Delivery
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle
Molecules 2017, 22(1), 34;

Spectroscopic Studies on the Molecular Ageing of Serum Albumin

School of Pharmacy with the Division of Laboratory Medicine in Sosnowiec, Medical University of Silesia, Chair and Department of Physical Pharmacy, Jagiellońska 4, 41-200 Sosnowiec, Poland
Author to whom correspondence should be addressed.
Academic Editors: Josef Jampilek and Atanas G. Atanasov
Received: 29 September 2016 / Revised: 21 December 2016 / Accepted: 23 December 2016 / Published: 27 December 2016
Full-Text   |   PDF [8104 KB, uploaded 27 December 2016]   |  


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. View Full-Text
Keywords: molecular ageing; serum albumin; metoprolol; second derivative; circular dichroism molecular ageing; serum albumin; metoprolol; second derivative; circular dichroism

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Chudzik, M.; Maciążek-Jurczyk, M.; Pawełczak, B.; Sułkowska, A. Spectroscopic Studies on the Molecular Ageing of Serum Albumin. Molecules 2017, 22, 34.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top