Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2.
Eur J Pharmacol
; 885: 173499, 2020 Oct 15.
Article
in English
| MEDLINE | ID: covidwho-959755
ABSTRACT
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) α-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.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Antiviral Agents
/
Protease Inhibitors
/
Cathepsin L
/
Food
/
Betacoronavirus
/
Lactoferrin
Type of study:
Experimental Studies
Language:
English
Journal:
Eur J Pharmacol
Year:
2020
Document Type:
Article
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