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. - 16:(2026), pp. 18060.1-18060.24. [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.
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s41598-026-46442-9.pdf
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