Design and characterization of BSA-mycophenolic acid nanocomplexes : Antiviral activity exploration
Copyright © 2024 Elsevier B.V. All rights reserved..
The interactions between bovine serum albumin (BSA) and mycophenolic acid (MPA) were investigated in silico through molecular docking and in vitro, using fluorescence spectroscopy. Dynamic light scattering and scanning electron microscopy were used to figure out the structure of MPA-Complex (MPA-C). The binding affinity between MPA and BSA was determined, yielding a Kd value of (12.0 ± 0.7) μM, and establishing a distance of 17 Å between the BSA and MPA molecules. The presence of MPA prompted protein aggregation, leading to the formation of MPA-C. The cytotoxicity of MPA-C and its ability to fight Junín virus (JUNV) were tested in A549 and Vero cell lines. It was found that treating infected cells with MPA-C decreased the JUNV yield and was more effective than free MPA in both cell line models for prolonged time treatments. Our results represent the first report of the antiviral activity of this type of BSA-MPA complex against JUNV, as assessed in cell culture model systems. MPA-C shows promise as a candidate for drug formulation against human pathogenic arenaviruses.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:265 |
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| Enthalten in: |
International journal of biological macromolecules - 265(2024), Pt 2 vom: 02. Apr., Seite 131023 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Castañeda Cataña, Mayra A [VerfasserIn] |
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| Links: |
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| Themen: |
27432CM55Q |
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| Anmerkungen: |
Date Completed 18.04.2024 Date Revised 18.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.ijbiomac.2024.131023 |
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NLM370034767 |
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| 245 | 1 | 0 | |a Design and characterization of BSA-mycophenolic acid nanocomplexes |b Antiviral activity exploration |
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| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2024 Elsevier B.V. All rights reserved. | ||
| 520 | |a The interactions between bovine serum albumin (BSA) and mycophenolic acid (MPA) were investigated in silico through molecular docking and in vitro, using fluorescence spectroscopy. Dynamic light scattering and scanning electron microscopy were used to figure out the structure of MPA-Complex (MPA-C). The binding affinity between MPA and BSA was determined, yielding a Kd value of (12.0 ± 0.7) μM, and establishing a distance of 17 Å between the BSA and MPA molecules. The presence of MPA prompted protein aggregation, leading to the formation of MPA-C. The cytotoxicity of MPA-C and its ability to fight Junín virus (JUNV) were tested in A549 and Vero cell lines. It was found that treating infected cells with MPA-C decreased the JUNV yield and was more effective than free MPA in both cell line models for prolonged time treatments. Our results represent the first report of the antiviral activity of this type of BSA-MPA complex against JUNV, as assessed in cell culture model systems. MPA-C shows promise as a candidate for drug formulation against human pathogenic arenaviruses | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Arenavirus | |
| 650 | 4 | |a Bovine serum albumin | |
| 650 | 4 | |a Mycophenolic acid | |
| 650 | 4 | |a Nanocomplexes | |
| 650 | 7 | |a Serum Albumin, Bovine |2 NLM | |
| 650 | 7 | |a 27432CM55Q |2 NLM | |
| 650 | 7 | |a Mycophenolic Acid |2 NLM | |
| 650 | 7 | |a HU9DX48N0T |2 NLM | |
| 650 | 7 | |a Antiviral Agents |2 NLM | |
| 700 | 1 | |a Dodes Traian, Martín M |e verfasserin |4 aut | |
| 700 | 1 | |a Rivas Marquina, Andrea P |e verfasserin |4 aut | |
| 700 | 1 | |a Marquez, Agostina B |e verfasserin |4 aut | |
| 700 | 1 | |a Arrúa, Eva C |e verfasserin |4 aut | |
| 700 | 1 | |a Carlucci, María J |e verfasserin |4 aut | |
| 700 | 1 | |a Damonte, Elsa B |e verfasserin |4 aut | |
| 700 | 1 | |a Pérez, Oscar E |e verfasserin |4 aut | |
| 700 | 1 | |a Sepúlveda, Claudia S |e verfasserin |4 aut | |
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