Templating α-amylase peptide inhibitors with organotin compounds

Fernando Porcelli, Cristina Olivieri, Larry R. Masterson, Yi Wang, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Metal centers have been widely used to nucleate secondary structures in linear peptides. However, very few examples have been reported for peptide/organometal complexes. Here, we illustrate the use of organotin compounds as nucleation centers for secondary structures of linear peptide inhibitors of α-amylase. Specifically, we utilized methyl-substituted tin compounds to template short type I β-turns similar to the binding loop of tendamistat, the natural inhibitor of the enzyme, which are able to bind and inhibit α-amylase. We show that enzyme activity is inhibited by neither the unstructured peptide nor the organotin compounds, but rather the peptide/organotin complex, which inhibits the enzyme with K i ~ 0.5 μM. The results delineate a strategy to use organometallic compounds to drive the active conformation in small linear peptides.

Original languageEnglish (US)
Pages (from-to)1197-1204
Number of pages8
JournalJournal of Biological Inorganic Chemistry
Issue number8
StatePublished - Dec 1 2011


  • Fluorescence spectroscopy
  • Inhibition
  • Organotin compounds
  • Stannin
  • α-Amylase


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