Exploring the impact of the side-chain length on peptide/RNA binding events.
| dc.rights.license | open | en_US |
| dc.contributor.author | SBICCA, Lola | |
| dc.contributor.author | GONZÁLEZ, Alejandro López | |
| dc.contributor.author | GRESIKA, Alexandra | |
| dc.contributor.author | DI GIORGIO, Audrey | |
| dc.contributor.author | CLOSA, Jordi Teixido | |
| dc.contributor.author | TEJEDOR, Roger Estrada | |
| hal.structure.identifier | Microbiologie Fondamentale et Pathogénicité [MFP] | |
| dc.contributor.author | ANDREOLA, Marie-Aline | |
| dc.contributor.author | AZOULAY, Stéphane | |
| dc.contributor.author | PATINO, Nadia | |
| dc.date.accessioned | 2023-11-08T13:18:20Z | |
| dc.date.available | 2023-11-08T13:18:20Z | |
| dc.date.issued | 2017-07-19 | |
| dc.identifier.issn | 1463-9084 | en_US |
| dc.identifier.uri | https://oskar-bordeaux.fr/handle/20.500.12278/184684 | |
| dc.description.abstractEn | The impact of the amino-acid side-chain length on peptide-RNA binding events has been investigated using HIV-1 Tat derived peptides as ligands and the HIV-1 TAR RNA element as an RNA model. Our studies demonstrate that increasing the length of all peptide side-chains improves unexpectedly the binding affinity (K) but reduces the degree of compactness of the peptide-RNA complex. Overall, the side-chain length appears to modulate in an unpredictable way the ability of the peptide to compete with the cognate TAR RNA partner. Beyond the establishment of non-intuitive fundamental relationships, our results open up new perspectives in the design of effective RNA ligand competitors, since a large number of them have already been identified but few studies report on the modulation of the biological activity by modifying in the same way the length of all chains connecting RNA recognition motives to the central scaffold of a ligand. | |
| dc.language.iso | EN | en_US |
| dc.subject.en | Amino Acid Sequence | |
| dc.subject.en | HIV Long Terminal Repeat | |
| dc.subject.en | HIV-1 | |
| dc.subject.en | Humans | |
| dc.subject.en | Molecular Dynamics Simulation | |
| dc.subject.en | Peptides | |
| dc.subject.en | Phase Transition | |
| dc.subject.en | Protein Binding | |
| dc.subject.en | RNA | |
| dc.subject.en | Viral | |
| dc.subject.en | Spectrophotometry | |
| dc.subject.en | Ultraviolet | |
| dc.subject.en | Spectroscopy | |
| dc.subject.en | Fourier Transform Infrared | |
| dc.subject.en | Temperature | |
| dc.subject.en | Thermodynamics | |
| dc.subject.en | Ultraviolet Rays | |
| dc.title.en | Exploring the impact of the side-chain length on peptide/RNA binding events. | |
| dc.title.alternative | Phys Chem Chem Phys | en_US |
| dc.type | Article de revue | en_US |
| dc.identifier.doi | 10.1039/c7cp03726k | en_US |
| dc.subject.hal | Sciences du Vivant [q-bio]/Microbiologie et Parasitologie | en_US |
| dc.identifier.pubmed | 28681892 | en_US |
| bordeaux.journal | Physical Chemistry Chemical Physics | en_US |
| bordeaux.page | 18452-18460 | en_US |
| bordeaux.volume | 19 | en_US |
| bordeaux.hal.laboratories | MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234 | en_US |
| bordeaux.issue | 28 | en_US |
| bordeaux.institution | CNRS | en_US |
| bordeaux.peerReviewed | oui | en_US |
| bordeaux.inpress | non | en_US |
| bordeaux.import.source | pubmed | |
| hal.identifier | hal-04275353 | |
| hal.version | 1 | |
| hal.date.transferred | 2023-11-08T13:18:23Z | |
| hal.popular | non | en_US |
| hal.audience | Internationale | en_US |
| hal.export | true | |
| workflow.import.source | pubmed | |
| dc.rights.cc | Pas de Licence CC | en_US |
| bordeaux.COinS | ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Physical%20Chemistry%20Chemical%20Physics&rft.date=2017-07-19&rft.volume=19&rft.issue=28&rft.spage=18452-18460&rft.epage=18452-18460&rft.eissn=1463-9084&rft.issn=1463-9084&rft.au=SBICCA,%20Lola&GONZ%C3%81LEZ,%20Alejandro%20L%C3%B3pez&GRESIKA,%20Alexandra&DI%20GIORGIO,%20Audrey&CLOSA,%20Jordi%20Teixido&rft.genre=article |
