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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

83.8K
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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Phosphodiester Linkages01:01

Phosphodiester Linkages

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Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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A study of 2-component i, i + 3 peptide stapling using thioethers.

Lauren E St Louis1, Tayliz M Rodriguez1, Marcey L Waters1

  • 1Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Bioorganic & Medicinal Chemistry
|November 11, 2017
PubMed
Summary

Peptide stapling stabilizes helical structures and enhances therapeutic potential. This study explores i, i+3 spacing for improved peptide stability and proteolytic resistance, outperforming traditional i, i+4 methods.

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Area of Science:

  • Biochemistry
  • Medicinal Chemistry
  • Drug Discovery

Background:

  • Peptides offer therapeutic potential for
  • undruggable
  • targets, but short peptides are unstable.
  • Peptide stapling enhances structural stability and protease resistance.

Purpose of the Study:

  • Evaluate bifunctional linkers for i, i+3 peptide stapling.
  • Compare the efficacy of i, i+3 vs. i, i+4 stapling for stability and protease resistance.

Main Methods:

  • Synthesized and tested various bifunctional linkers for i, i+3 stapling.
  • Assessed peptide helicity and reactivity with linkers.
  • Measured peptide half-life in cell lysates to evaluate proteolytic resistance.

Main Results:

  • Identified effective bifunctional linkers for i, i+3 peptide stapling.
  • Demonstrated increased helicity and stability with i, i+3 stapling.
  • Showed i, i+3 stapling significantly enhanced peptide half-life compared to i, i+4 stapling.

Conclusions:

  • i, i+3 peptide stapling is an effective strategy to enhance peptide stability and therapeutic potential.
  • This method expands the peptide stapling toolbox for drug development.