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.| File | Dimensione | Formato | |
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s41598-026-46442-9_reference.pdf
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2.84 MB | Adobe PDF |
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