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. Author manuscript; available in PMC: 2022 Jul 6.
Published in final edited form as: Sci Transl Med. 2022 May 25;14(646):eabn1252. doi: 10.1126/scitranslmed.abn1252

Fig 1. Multivalent minibinders exhibit very slow dissociation rates upon binding to the prefusion SARS-CoV-2-S glycoprotein trimer.

Fig 1.

Dissociation of the minibinder construct was monitored by competition with 100-fold molar excess of untagged MON1 using AlphaLISA (Mean ± SEM, n = 3 technical replicates from a single experiment). (A) Dissociation was measured for indicated minibinder constructs complexed with the receptor-binding domain of SARS-CoV-2 (RBD). (B) Dissociation was measured for the indicated minibinder constructs complexed with the S trimer (S6P).