The B.1.1.7 SARS-CoV-2 strain that has emerged in the UK in early December presents seven mutations and three deletions on S-protein structure that could lead to a more infective strain. The P681H mutation in the “PRRAR” furin cleavage site might affect the binding affinity to furin enzyme and hence its infectivity.

Therefore, in this study, various structural bioinformatics approaches were used to model the S-protein structure with the B.1.1.7 variant amino acid substitutions and deletions. In addition to modelling the binding of furin to the cleavage site of the wild-type and the B.1.1.7 variant.

Conclusively the B.1.1.7 variant resulted in dynamic stability, conformational changes and variations in binding energies in the S-protein structure, resulting in a more favourable binding of furin enzyme to the SARS-CoV-2 S-protein.

12 月初在英国出现的 B.1.1.7 SARS-CoV-2 毒株在 S 蛋白结构上出现了 7 个突变和 3 个缺失，这可能会导致感染性更强的毒株。“PRRAR”弗林蛋白酶切割位点中的 P681H 突变可能会影响与弗林蛋白酶的结合亲和力，从而影响其传染性。

因此，在本研究中，使用各种结构生物信息学方法对具有 B.1.1.7 变体氨基酸取代和缺失的 S 蛋白结构进行建模。除了模拟弗林蛋白酶与野生型和 B.1.1.7 变体的切割位点的结合。

最终，B.1.1.7 变体导致 S 蛋白结构中的动态稳定性、构象变化和结合能的变化，从而导致弗林蛋白酶更有利地与 SARS-CoV-2 S 蛋白结合。