Food proteins are a potential resource for mining cathepsin L inhibitory drugs to combat SARS-CoV-2

Ashkan Madadlou*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Scopus)

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.

Original languageEnglish
Article number173499
JournalEuropean Journal of Pharmacology
Volume885
DOIs
Publication statusPublished - 15 Oct 2020

Keywords

  • COVID-19
  • Food
  • Infection
  • Lactoferrin
  • Protein
  • Virus

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