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The entry of SARS-CoV-2 into host cells proceeds by a proteolysis process, which involves the lysosomal peptidase cathepsin L Inhibition of cathepsin L is therefore considered an effective method to decrease the virus internalization Analysis from the perspective of structure-functionality elucidates that cathepsin L inhibitory proteins/peptides found in food share specific features: multiple disulfide crosslinks (buried in protein core), lack or low contents of (small) a-helices, and high surface hydrophobicity Lactoferrin can inhibit cathepsin L, but not cathepsins B and H This selective inhibition might be useful in fine targeting of cathepsin L Molecular docking indicated that only the carboxyl-terminal lobe of lactoferrin interacts with cathepsin L and that the active site cleft of cathepsin L is heavily superposed by lactoferrin A controlled proteolysis process might yield lactoferrin-derived peptides that strongly inhibit cathepsin L
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European_Journal_of_Pharmacology
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Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2. (Special Issue: Therapeutic targets and pharmacological treatment of COVID-19.)
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