Cyclic Peptide-Based Sirtuin Substrates

Peptide ormosils as cellular substrates

Mechanism-based sirtuin enzyme activation

Sirtuin enzymes are NAD-dependent protein deacylases that play a central role in the regulation of healthspan and lifespan in organisms ranging from yeast to mammals. There is intense interest in the activation of the seven mammalian sirtuins (SIRT1-7) in order to extend mammalian healthspan and lifespan. However, there is currently no understanding of how to design sirtuin-activating compounds...

A succinyl lysine-based photo-cross-linking peptide probe for Sirtuin 5.

A succinylation-specific photo-cross-linking peptide probe has been developed for the NAD(+)-dependent hydrolase Sirtuin 5. The probe, not only displayed robust labelling performance with purified Sirt5, but also enabled sensitive detection of the hydrolase in the presence of large excess of cellular proteins. It is anticipated that this probe, and future generations of it, will provide useful ...

A cyclic peptide-based redox-active model of rubredoxin.

A model of rubredoxin based on a cyclic peptide with a linear tail is presented. This model reproduces almost perfectly the fold, the spectroscopic characterizations and the redox activity of rubredoxins.

Peptidase Substrates via Global Peptide Profiling

Peptide metabolism is a complex process that involves many proteins working in concert. Mass spectrometry-based global peptide profiling of mice lacking dipeptidyl peptidase 4 (DPP4) identified endogenous DPP4 substrates and revealed an unrecognized pathway during proline peptide catabolism that interlinks aminopeptidase and DPP4 activities. Together, these studies elucidate specific aspects of...