This article explores synthetic peptide ligands targeting the intrinsically disordered regions of the SARS-CoV-2 nucleocapsid protein. Using NMR spectroscopy, molecular dynamics, and circular dichroism, the study shows how peptide sequence and flexibility influence binding affinity. The results support a modular peptide design strategy for targeting complex proteins, with potential applications in antiviral research.

Peptide ligands to explore interactions with intrinsically disordered multidomain proteins: the case of SARS-CoV-2 nucleocapsid protein / Tino, A. S.; Quagliata, M.; Schiavina, M.; Attanasio, L.; Santos, B. P. O.; Pacini, L.; Papini, A. M.; Pierattelli, R.; Felli, I. C.. - In: SCIENTIFIC REPORTS. - ISSN 2045-2322. - ELETTRONICO. - (2026), pp. 0-0. [10.1038/s41598-026-46442-9]

Peptide ligands to explore interactions with intrinsically disordered multidomain proteins: the case of SARS-CoV-2 nucleocapsid protein

Tino, A. S.
;
Quagliata, M.
;
Schiavina, M.
;
Papini, A. M.
;
Pierattelli, R.
;
Felli, I. C.
2026

Abstract

This article explores synthetic peptide ligands targeting the intrinsically disordered regions of the SARS-CoV-2 nucleocapsid protein. Using NMR spectroscopy, molecular dynamics, and circular dichroism, the study shows how peptide sequence and flexibility influence binding affinity. The results support a modular peptide design strategy for targeting complex proteins, with potential applications in antiviral research.
2026
0
0
Tino, A. S.; Quagliata, M.; Schiavina, M.; Attanasio, L.; Santos, B. P. O.; Pacini, L.; Papini, A. M.; Pierattelli, R.; Felli, I. C.
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1468386
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