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Peptide Bonds

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

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Related Experiment Video

Updated: Jan 30, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

Cyclic Peptide-Based Sirtuin Substrates.

Di Chen¹, Lingling Yan², Weiping Zheng³

¹School of Pharmacy, Jiangsu University, 301 Xuefu Road, Zhenjiang 212013, China. jsdxchendi@163.com.

Molecules (Basel, Switzerland)

|January 27, 2019

Summary

Researchers identified novel cyclic peptides as effective substrates for human SIRT1, SIRT2, and SIRT3 enzymes. These peptides demonstrate good substrate activity in deacylation reactions, indicating potential roles in enzymatic studies.

Keywords:

cyclic peptide deacylation sirtuin substrate

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Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

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Published on: February 27, 2016

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Construction of Cyclic Cell-Penetrating Peptides for Enhanced Penetration of Biological Barriers

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Published on: September 19, 2022

Area of Science:

Biochemistry
Enzymology
Molecular Biology

Background:

Sirtuins (SIRTs) are a class of NAD+-dependent deacetylases and deacylases involved in various cellular processes.
Understanding the substrate specificity of human SIRT1, SIRT2, and SIRT3 is crucial for developing targeted therapeutics and biochemical tools.
Cyclic peptides offer unique structural scaffolds for studying enzyme-substrate interactions.

Purpose of the Study:

To investigate the in vitro substrate activities of novel cyclic peptides against human SIRT1, SIRT2, and SIRT3.
To characterize the deacylation of Nε-acetyl-lysine and Nε-myristoyl-lysine containing cyclic peptides by sirtuins.

Main Methods:

Synthesis of four side chain-to-side chain cyclic peptides (three 5-mers and one 4-mer) containing modified lysine residues.
In vitro enzymatic assays to measure the deacylation activity of purified human SIRT1, SIRT2, and SIRT3.
Determination of kinetic parameters (kcat/KM) to quantify substrate activity.

Main Results:

Four cyclic peptides, including three 5-mers and one 4-mer, were synthesized and characterized.
All tested cyclic peptides, featuring Nε-acetyl-lysine or Nε-myristoyl-lysine, exhibited good substrate activities.
Enzymatic deacylation by human SIRT1, SIRT2, and SIRT3 was confirmed, as indicated by favorable kcat/KM ratios.

Conclusions:

Novel cyclic peptides are effective in vitro substrates for human SIRT1, SIRT2, and SIRT3.
These findings provide valuable insights into the substrate specificity of sirtuins.
The characterized peptides may serve as useful tools for further biochemical and pharmacological studies of sirtuin activity.