Journal
FUTURE MEDICINAL CHEMISTRY
Volume 11, Issue 1, Pages 5-19Publisher
FUTURE SCI LTD
DOI: 10.4155/fmc-2018-0216
Keywords
arginine; enzyme inhibition; obesity; pancreatic lipase; tripeptides
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Funding
- Ministry of Education, University, and Research of Italy (University 'Gabriele d'Annunzio' University of Chieti-Pescara, FAR 2017)
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Aim: The inhibition of pancreatic lipase (PL) represents one of the most promising strategies in the search for novel antiobesity drugs. We propose here a pioneering course by exploring tripeptide scaffolds in the way to selective PL inhibitors. Methodology/Results: The peptide series exhibited good PL inhibitory properties in vitro, with all the strongest inhibitors sharing a central arginine, shown in silico to be relevant for the active site-directed activity. The compounds were found devoid of inhibitory properties on acetylcholinesterase. Conclusion: Present results disclosed that basic tripeptides are able to interact efficiently with the PL-binding pocket, where they adopt a binding pose suitable for functional-to-inhibition interactions with key amino acids. Main inhibitor MALA4 may be selected as lead for further optimization.
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