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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

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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In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Published on: January 26, 2016

Dicyclopropylmethyl peptide backbone protectant.

Louis A Carpino1, Khaled Nasr, Adel Ali Abdel-Maksoud

  • 1Department of Chemistry, University of Massachusetts, Amherst, Massachusetts 01003, USA. carpino@chem.umass.edu

Organic Letters
|September 2, 2009
PubMed
Summary

The N-dicyclopropylmethyl (Dcpm) residue offers a novel amide bond protection strategy for peptide synthesis, effectively reducing aggregation. This method enhances the creation of complex peptides, including the prion peptide.

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Area of Science:

  • Organic Chemistry
  • Biochemistry
  • Peptide Synthesis

Background:

  • Amide bond protection is crucial in peptide synthesis to prevent unwanted side reactions.
  • Aggregation during peptide synthesis can significantly reduce yield and purity.
  • Existing protecting groups may not effectively address challenges like cyclization in sensitive sequences.

Purpose of the Study:

  • To introduce and evaluate the N-dicyclopropylmethyl (Dcpm) residue as an amide bond protectant in peptide synthesis.
  • To demonstrate the efficacy of the Dcpm group in mitigating aggregation during peptide assembly.
  • To show the utility of the Dcpm group in handling sensitive amino acid sequences, such as those containing Asp-Gly units.

Main Methods:

  • Introduction of the N-dicyclopropylmethyl (Dcpm) residue into amino acids using dicyclopropylmethanimine hydrochloride and subsequent reduction.
  • Application of the Dcpm-protected amino acids in solid-phase peptide synthesis.
  • Synthesis of model peptides, including an alanine decapeptide and the prion peptide (106-126), to assess aggregation effects.
  • Substitution of Fmoc-(Dcpm)Gly-OH for Fmoc-Gly-OH to evaluate protection against aminosuccinimide formation.

Main Results:

  • The N-dicyclopropylmethyl (Dcpm) residue successfully functions as an amide bond protectant in peptide synthesis.
  • The use of the Dcpm residue significantly ameliorated aggregation effects during the synthesis of model peptides.
  • Employing Fmoc-(Dcpm)Gly-OH prevented cyclization to aminosuccinimide in sequences with the sensitive Asp-Gly unit.

Conclusions:

  • The N-dicyclopropylmethyl (Dcpm) residue is a valuable tool for amide bond protection in peptide synthesis.
  • Dcpm protection effectively suppresses aggregation, leading to improved synthesis outcomes.
  • This protecting group strategy offers a solution for assembling peptides containing challenging sequences like Asp-Gly.