Cyclic Peptide-Based Sirtuin Substrates

Molecules. 2019 Jan 24;24(3):424. doi: 10.3390/molecules24030424.

Abstract

In the current study, four side chain-to-side chain cyclic peptides (three 5-mers and one 4-mer) harboring Nε-acetyl-lysine or Nε-myristoyl-lysine were found to be in vitro substrates of the human SIRT1/2/3-catalyzed deacylation with good substrate activities, as judged by the kcat/KM ratios.

Keywords: cyclic peptide; deacylation; sirtuin; substrate.

MeSH terms

  • Acylation
  • Catalysis
  • Humans
  • Kinetics
  • Lysine / analogs & derivatives
  • Lysine / chemistry
  • Molecular Structure
  • Oxidation-Reduction
  • Peptides, Cyclic / chemistry*
  • Pronase / metabolism
  • Sirtuins / chemistry*
  • Structure-Activity Relationship
  • Thermodynamics

Substances

  • Peptides, Cyclic
  • Pronase
  • Sirtuins
  • Lysine