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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
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. |
format | Online Article Text |
id | pubmed-7038104 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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