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Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding

Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the organism. Depending on the environment’s pH conditions, HSA can take one of the five isomeric forms that change its conformation. HSA can form aggregates resembling those in vitro formed from amyloid at physiologi...

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Autores principales: Maciążek-Jurczyk, Małgorzata, Janas, Kamil, Pożycka, Jadwiga, Szkudlarek, Agnieszka, Rogóż, Wojciech, Owczarzy, Aleksandra, Kulig, Karolina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7038104/
https://www.ncbi.nlm.nih.gov/pubmed/32023900
http://dx.doi.org/10.3390/molecules25030618
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author Maciążek-Jurczyk, Małgorzata
Janas, Kamil
Pożycka, Jadwiga
Szkudlarek, Agnieszka
Rogóż, Wojciech
Owczarzy, Aleksandra
Kulig, Karolina
author_facet Maciążek-Jurczyk, Małgorzata
Janas, Kamil
Pożycka, Jadwiga
Szkudlarek, Agnieszka
Rogóż, Wojciech
Owczarzy, Aleksandra
Kulig, Karolina
author_sort Maciążek-Jurczyk, Małgorzata
collection PubMed
description Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the organism. Depending on the environment’s pH conditions, HSA can take one of the five isomeric forms that change its conformation. HSA can form aggregates resembling those in vitro formed from amyloid at physiological pH (neutral and acidic). Not surprisingly, the main goal of the research was aggregation/fibrillation of HSA, the study of the physicochemical properties of formed amyloid fibrils using thioflavin T (ThT) and the analysis of ligand binding to aggregated/fibrillated albumin in the presence of dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), phenylbutazone (Phb) and ketoprofen (Ket). Solutions of human serum albumin, both non-modified and modified, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. The experiments conducted allowed observation of changes in the structure of incubated HSA (HSA(INC)) in relation to nonmodified HSA (HSA(FR)). The formed aggregates/fibrillation differed in structure from HSA monomers and dimers. Based on CD spectroscopy, previously absent β-structural constructs have been registered. Whereas, using fluorescence spectroscopy, the association constants differing for fresh and incubated HSA solutions in the presence of dansyl-amino acids and markers for binding sites were calculated and allowed observation of the conformational changes in HSA molecule.
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spelling pubmed-70381042020-03-10 Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding Maciążek-Jurczyk, Małgorzata Janas, Kamil Pożycka, Jadwiga Szkudlarek, Agnieszka Rogóż, Wojciech Owczarzy, Aleksandra Kulig, Karolina Molecules Article Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the organism. Depending on the environment’s pH conditions, HSA can take one of the five isomeric forms that change its conformation. HSA can form aggregates resembling those in vitro formed from amyloid at physiological pH (neutral and acidic). Not surprisingly, the main goal of the research was aggregation/fibrillation of HSA, the study of the physicochemical properties of formed amyloid fibrils using thioflavin T (ThT) and the analysis of ligand binding to aggregated/fibrillated albumin in the presence of dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), phenylbutazone (Phb) and ketoprofen (Ket). Solutions of human serum albumin, both non-modified and modified, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. The experiments conducted allowed observation of changes in the structure of incubated HSA (HSA(INC)) in relation to nonmodified HSA (HSA(FR)). The formed aggregates/fibrillation differed in structure from HSA monomers and dimers. Based on CD spectroscopy, previously absent β-structural constructs have been registered. Whereas, using fluorescence spectroscopy, the association constants differing for fresh and incubated HSA solutions in the presence of dansyl-amino acids and markers for binding sites were calculated and allowed observation of the conformational changes in HSA molecule. MDPI 2020-01-31 /pmc/articles/PMC7038104/ /pubmed/32023900 http://dx.doi.org/10.3390/molecules25030618 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Maciążek-Jurczyk, Małgorzata
Janas, Kamil
Pożycka, Jadwiga
Szkudlarek, Agnieszka
Rogóż, Wojciech
Owczarzy, Aleksandra
Kulig, Karolina
Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
title Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
title_full Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
title_fullStr Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
title_full_unstemmed Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
title_short Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
title_sort human serum albumin aggregation/fibrillation and its abilities to drugs binding
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7038104/
https://www.ncbi.nlm.nih.gov/pubmed/32023900
http://dx.doi.org/10.3390/molecules25030618
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