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10.1021/acsmedchemlett.0c00386

http://scihub22266oqcxt.onion/10.1021/acsmedchemlett.0c00386
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33738063!7957945!33738063
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suck abstract from ncbi


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pmid33738063      ACS+Med+Chem+Lett 2021 ; 12 (3): 365-372
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  • Design and Structure-Activity Relationship of a Potent Furin Inhibitor Derived from Influenza Hemagglutinin #MMPMID33738063
  • Lewandowska-Goch MA; Kwiatkowska A; Lepek T; Ly K; Navals P; Gagnon H; Dory YL; Prahl A; Day R
  • ACS Med Chem Lett 2021[Mar]; 12 (3): 365-372 PMID33738063show ga
  • Furin plays an important role in various pathological states, especially in bacterial and viral infections. A detailed understanding of the structural requirements for inhibitors targeting this enzyme is crucial to develop new therapeutic strategies in infectious diseases, including an urgent unmet need for SARS-CoV-2 infection. Previously, we have identified a potent furin inhibitor, peptide Ac-RARRRKKRT-NH (2) (CF1), based on the highly pathogenic avian influenza hemagglutinin. The goal of this study was to determine how its N-terminal part (the P8-P5 positions) affects its activity profile. To do so, the positional-scanning libraries of individual peptides modified at the selected positions with natural amino acids were generated. Subsequently, the best substitutions were combined together and/or replaced by unnatural residues to expand our investigations. The results reveal that the affinity of CF1 can be improved (2-2.5-fold) by substituting its P5 position with the small hydrophobic residues (Ile or Val) or a basic Lys.
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