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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...
Preparation of 1° Amines: Azide Synthesis01:22

Preparation of 1° Amines: Azide Synthesis

Direct alkylation of ammonia produces polyalkylated amines, along with a quaternary ammonium salt. To exclusively prepare primary amines, the azide synthesis method can be used.
Azide ions act as good nucleophiles and react with unhindered alkyl halides to form alkyl azides. Alkyl azides do not participate in further nucleophilic substitution reactions, thereby eliminating the chances of polyalkylated products. Alkyl azides are reduced by hydride-based reducing agents, like lithium aluminum...

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Synthesis and Structure Determination of &#181;-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
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Oxyazapeptides: synthesis, structure determination, and conformational analysis.

Suvendu Biswas1, Nader E Abo-Dya, Alexander Oliferenko

  • 1Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, Florida 32611-7200, USA.

The Journal of Organic Chemistry
|July 26, 2013
PubMed
Summary
This summary is machine-generated.

Researchers created novel oxyazapeptides by replacing a native N-C(α) bond with an O-N(α) bond. These stable peptidomimetics exhibit unique conformational properties and may aid drug discovery.

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Published on: August 1, 2018

Area of Science:

  • Medicinal Chemistry
  • Organic Chemistry
  • Structural Biology

Background:

  • Peptidomimetics are crucial in drug discovery for mimicking peptide structures.
  • Native peptide bonds are susceptible to hydrolysis, limiting their therapeutic applications.
  • Azapeptides offer improved stability but have specific conformational constraints.

Purpose of the Study:

  • To synthesize and characterize a new class of peptidomimetics, termed oxyazapeptides.
  • To investigate the hydrolytic stability and conformational behavior of oxyazapeptides.
  • To explore the potential of oxyazapeptides in drug discovery and biologics design.

Main Methods:

  • Synthesis of novel oxyazapeptide compounds.
  • X-ray structure determination for structural insights.
  • Force field calculations for conformational analysis.
  • Comparison with azapeptides and native peptides.

Main Results:

  • Successful synthesis of a novel class of oxyazapeptides.
  • Oxyazapeptides demonstrate significant hydrolytic stability.
  • The O-N(α) bond exhibits a five-fold lower rotational barrier compared to the N-N(α) bond in azapeptides.
  • Conformational analysis indicates the propensity of the oxyaza moiety to induce β-turns.

Conclusions:

  • Oxyazapeptides represent a new family of peptidomimetics with enhanced stability.
  • The unique conformational properties, including β-turn induction, make oxyazapeptides promising scaffolds.
  • This novel scaffold holds potential for advancing drug discovery and the design of biologics.