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• W4382199522 abstract "The Spike protein (S1) from the Severe acute respiratory syndrome 2 virus binds to angiotensin converting enzyme 2 (ACE2) receptor to initiate infection. Hence, antiviral therapeutic targeting the S1-ACE2 interface is of interest. Herein, we compare the inhibition efficacy of an aptamer to heparin or their cocktail, against wild-type (WT), Omicron, Delta, and Lambda S1-ACE2 complexes. The aptamer-protein complexes had the dissociation constant KD values in the 2-13 nM range. The aptamer half-maximal inhibitory concentration against WT S1-ACE was 17 nM, with the % inhibition in the 12-35% range. Several aptamer-S1 protein complexes were also stable at low pH with 60% inhibition. Despite the similarity in S1 sequences, the extent of inhibition (2-27%) with heparin was highly dependent on the type of S1 protein. More importantly, heparin did not inhibit the WT S1-ACE2 complex but was effective with mutants. The aptamer-heparin cocktail was less effective compared to aptamer or heparin, individually. Modelling data show that either a direct or proximal binding to RBD sites by aptamer or heparin prevents the ACE2 binding. Overall, heparin was as an effective inhibitor as aptamer against certain variants, and represents the more cost-effective neutralizing agent against emerging coronaviruses." @default.
• W4382199522 created "2023-06-28" @default.
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• W4382199522 date "2023-09-01" @default.
• W4382199522 modified "2023-10-12" @default.
• W4382199522 title "Aptamer-, heparin- or cocktail-based inhibition of S1-ACE2 protein complexes" @default.
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• W4382199522 doi "https://doi.org/10.1016/j.ab.2023.115223" @default.
• W4382199522 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37385465" @default.
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