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Dimeric and monomeric conformation of SARS-CoV-2 main protease: New technical approaches based on IR radiation.
Piccirilli, Federica; Vondracek, Hendrik; Silvestrini, Lucia; Parisse, Pietro; Spinozzi, Francesco; Vaccari, Lisa; Toma, Andrea; Aglieri, Vincenzo; Casalis, Loredana; Piccionello, Antonio Palumbo; Mariani, Paolo; Birarda, Giovanni; Ortore, Maria Grazia.
Afiliación
  • Piccirilli F; AREA Science Park, Padriciano 99, Trieste, I- 34149, Italy.
  • Vondracek H; Elettra-Synchrotron Trieste S.C.p.A., Strada Statale 14, Basovizza, Trieste, I-34149, Italy.
  • Silvestrini L; Department of Life and Environmental Sciences, Marche Polytechnic University, via brecce bianche, Ancona, I-60131, Italy.
  • Parisse P; Elettra-Synchrotron Trieste S.C.p.A., Strada Statale 14, Basovizza, Trieste, I-34149, Italy; CNR - Istituto Officina dei Materiali, s.s. 14 km 163.5 in Area Science Park, 34149 Basovizza, Trieste, Italy.
  • Spinozzi F; Department of Life and Environmental Sciences, Marche Polytechnic University, via brecce bianche, Ancona, I-60131, Italy.
  • Vaccari L; Elettra-Synchrotron Trieste S.C.p.A., Strada Statale 14, Basovizza, Trieste, I-34149, Italy.
  • Toma A; Fondazione Istituto Italiano di Tecnologia, via Morego 30, Genova, I- 16163, Italy.
  • Aglieri V; Fondazione Istituto Italiano di Tecnologia, via Morego 30, Genova, I- 16163, Italy.
  • Casalis L; Elettra-Synchrotron Trieste S.C.p.A., Strada Statale 14, Basovizza, Trieste, I-34149, Italy.
  • Piccionello AP; Dipartimento di Scienze e Tecnologie Biologiche Chimiche e Farmaceutiche, viale delle scienze, Palermo, I-90133, Italy.
  • Mariani P; Department of Life and Environmental Sciences, Marche Polytechnic University, via brecce bianche, Ancona, I-60131, Italy.
  • Birarda G; Elettra-Synchrotron Trieste S.C.p.A., Strada Statale 14, Basovizza, Trieste, I-34149, Italy. Electronic address: giovanni.birarda@elettra.eu.
  • Ortore MG; Department of Life and Environmental Sciences, Marche Polytechnic University, via brecce bianche, Ancona, I-60131, Italy. Electronic address: m.g.ortore@univpm.it.
Spectrochim Acta A Mol Biomol Spectrosc ; 322: 124772, 2024 Dec 05.
Article en En | MEDLINE | ID: mdl-39003826
ABSTRACT
The main proteases Mpro are a group of highly conserved cysteine hydrolases in ß-coronaviruses. They have been demonstrated to play an unavoidable role in viral replication, and consequently they have been suggested as key targets for treating coronavirus-caused infectious diseases, mainly from the COVID-19 epidemic. Since the most functional form for Mpro enzymatic activity is associated to its homodimer, compounds inhibiting dimerization should also inhibit catalytic activity. We show how PIR-SEIRA (Plasmonic Internal Reflection-Surface Enhanced InfraRed Absorption) spectroscopy can be a noteworthy technique to study proteins subtle structural variations associated to inhibitor binding. Nanoantennas arrays can selectively confine and enhance electromagnetic field via localized plasmonic resonances, thus promoting ultrasensitive detection of biomolecules in close proximity of nanoantenna arrays and enabling the effective investigation of protein monolayers. By adopting this approach, reflection measurements conducted under back illumination of nanoantennas allow to probe anchored protein monolayers, with minimum contribution of environmental buffer molecules. PIR-SEIRA spectroscopy on Mpro was carried out by ad hoc designed devices, resonating in the spectral region of Amide I and Amide II bands. We evaluated here the structure of anchored monomers and dimers in different buffered environment and in presence of a newly designed Mpro inhibitor. Experimental results show that dimerization is not associated to relevant backbone rearrangements of the protein at secondary structure level, and even if the compound inhibits the dimerization, it is not effective at breaking preformed dimers.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espectrofotometría Infrarroja / Proteasas 3C de Coronavirus / SARS-CoV-2 Límite: Humans Idioma: En Revista: Spectrochim Acta A Mol Biomol Spectrosc Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Espectrofotometría Infrarroja / Proteasas 3C de Coronavirus / SARS-CoV-2 Límite: Humans Idioma: En Revista: Spectrochim Acta A Mol Biomol Spectrosc Asunto de la revista: BIOLOGIA MOLECULAR Año: 2024 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Reino Unido