ArticleMolecules (Basel, Switzerland)2016
Spectroscopic Studies on the Molecular Ageing of Serum Albumin.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 45 citations in OpenAlex.
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- Ligand-human serum albumin analysis: the near-UV CD and UV-Vis spectroscopic studies.Naunyn-Schmiedeberg's archives of pharmacology · 2025Article
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- Ultraviolet Resonance Raman Spectra of Serum Albumins.Applied spectroscopy · 2023Article
- Interaction of Ibuprofen with Partially Unfolded Bovine Serum Albumin in the Presence of Ionic Micelles and Oligosaccharides at Different λACS omega · 2023Article
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- Spectroscopic Analysis of an Antimalarial Drug's (Quinine) Influence on Human Serum Albumin Reduction and Antioxidant Potential.Molecules (Basel, Switzerland) · 2022Article
- Biochemical Properties of Atranorin-Induced Behavioral and Systematic Changes of Laboratory Rats.Life (Basel, Switzerland) · 2022Article
- Interaction study of monoisoamyl dimercaptosuccinic acid with bovine serum albumin using biophysical and molecular docking approaches.Scientific reports · 2021Article
- Buffer effects on protein sieving losses in ultrafiltration and their relationship to biophysical properties.Biotechnology progressArticle
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.