Human Serum Albumin Aggregation/Fibrillation and its Abilities to Drugs Binding
| Autor: | Agnieszka Szkudlarek, Karolina Kulig, Jadwiga Pożycka, Wojciech Rogóż, M. Maciążek-Jurczyk, Kamil Janas, Aleksandra Owczarzy |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Circular dichroism
Pharmaceutical Science 02 engineering and technology Ligands Analytical Chemistry chemistry.chemical_compound Drug Discovery Dansyl Compounds aggregation/fibrillation 0303 health sciences spectroscopic methods 021001 nanoscience & nanotechnology Human serum albumin Phenylbutazone Ketoprofen human serum albumin Chemistry (miscellaneous) embryonic structures Molecular Medicine Thioflavin 0210 nano-technology Protein Binding medicine.drug Amyloid Proline Serum Albumin Human complex mixtures Article Fluorescence Fluorescence spectroscopy lcsh:QD241-441 03 medical and health sciences lcsh:Organic chemistry Prohibitins medicine Humans Physical and Theoretical Chemistry Binding site 030304 developmental biology Binding Sites Organic Chemistry Albumin equipment and supplies In vitro body regions Kinetics chemistry Biophysics bacteria |
| Zdroj: | Molecules, Vol 25, Iss 3, p 618 (2020) Molecules Volume 25 Issue 3 |
| ISSN: | 1420-3049 |
| Popis: | Human serum albumin (HSA) is a protein that transports neutral and acid ligands in the organism. Depending on the environment&rsquo 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 (HSAINC) in relation to nonmodified HSA (HSAFR). The formed aggregates/fibrillation differed in structure from HSA monomers and dimers. Based on CD spectroscopy, previously absent &beta 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. |
| Databáze: | OpenAIRE |
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