Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence
This study investigated the interaction between Human Serum Albumin (HSA) and microRNA 155 (miR-155) through spectroscopic, nanoscopic and computational methods. Atomic force spectroscopy together with static and time-resolved fluorescence demonstrated the formation of an HSA/miR-155 complex charact...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-09-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/18/10728 |
| _version_ | 1797487212240044032 |
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| author | Valentina Botti Salvatore Cannistraro Anna Rita Bizzarri |
| author_facet | Valentina Botti Salvatore Cannistraro Anna Rita Bizzarri |
| author_sort | Valentina Botti |
| collection | DOAJ |
| description | This study investigated the interaction between Human Serum Albumin (HSA) and microRNA 155 (miR-155) through spectroscopic, nanoscopic and computational methods. Atomic force spectroscopy together with static and time-resolved fluorescence demonstrated the formation of an HSA/miR-155 complex characterized by a moderate affinity constant (K<sub>A</sub> in the order of 10<sup>4</sup> M<sup>−1</sup>). Förster Resonance Energy Transfer (FRET) experiments allowed us to measure a distance of (3.9 ± 0.2) nm between the lone HSA Trp214 and an acceptor dye bound to miR-155 within such a complex. This structural parameter, combined with computational docking and binding free energy calculations, led us to identify two possible models for the structure of the complex, both characterized by a topography in which miR-155 is located within two positively charged pockets of HSA. These results align with the interaction found for HSA and miR-4749, reinforcing the thesis that native HSA is a suitable miRNA carrier under physiological conditions for delivering to appropriate targets. |
| first_indexed | 2024-03-09T23:44:23Z |
| format | Article |
| id | doaj.art-fded308d7e4b43d2b9942c709ca169ae |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T23:44:23Z |
| publishDate | 2022-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-fded308d7e4b43d2b9942c709ca169ae2023-11-23T16:47:00ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-09-0123181072810.3390/ijms231810728Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling EvidenceValentina Botti0Salvatore Cannistraro1Anna Rita Bizzarri2Biophysics and Nanoscience Centre, DEB, Università della Tuscia, Largo dell’Università, 01100 Viterbo, ItalyBiophysics and Nanoscience Centre, DEB, Università della Tuscia, Largo dell’Università, 01100 Viterbo, ItalyBiophysics and Nanoscience Centre, DEB, Università della Tuscia, Largo dell’Università, 01100 Viterbo, ItalyThis study investigated the interaction between Human Serum Albumin (HSA) and microRNA 155 (miR-155) through spectroscopic, nanoscopic and computational methods. Atomic force spectroscopy together with static and time-resolved fluorescence demonstrated the formation of an HSA/miR-155 complex characterized by a moderate affinity constant (K<sub>A</sub> in the order of 10<sup>4</sup> M<sup>−1</sup>). Förster Resonance Energy Transfer (FRET) experiments allowed us to measure a distance of (3.9 ± 0.2) nm between the lone HSA Trp214 and an acceptor dye bound to miR-155 within such a complex. This structural parameter, combined with computational docking and binding free energy calculations, led us to identify two possible models for the structure of the complex, both characterized by a topography in which miR-155 is located within two positively charged pockets of HSA. These results align with the interaction found for HSA and miR-4749, reinforcing the thesis that native HSA is a suitable miRNA carrier under physiological conditions for delivering to appropriate targets.https://www.mdpi.com/1422-0067/23/18/10728human serum albuminmiR-155AFSfluorescence quenchingFRETcomputational docking |
| spellingShingle | Valentina Botti Salvatore Cannistraro Anna Rita Bizzarri Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence International Journal of Molecular Sciences human serum albumin miR-155 AFS fluorescence quenching FRET computational docking |
| title | Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence |
| title_full | Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence |
| title_fullStr | Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence |
| title_full_unstemmed | Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence |
| title_short | Interaction of miR-155 with Human Serum Albumin: An Atomic Force Spectroscopy, Fluorescence, FRET, and Computational Modelling Evidence |
| title_sort | interaction of mir 155 with human serum albumin an atomic force spectroscopy fluorescence fret and computational modelling evidence |
| topic | human serum albumin miR-155 AFS fluorescence quenching FRET computational docking |
| url | https://www.mdpi.com/1422-0067/23/18/10728 |
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