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Peptide Bonds02:43

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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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight.  Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Structure and Function of AApeptides.

Olapeju Bolarinwa1, Alekhya Nimmagadda1, Ma Su1

  • 1Department of Chemistry, University of South Florida , 4202 East Fowler Avenue, Tampa, Florida 33620, United States.

Biochemistry
|December 29, 2016
PubMed
Summary

Researchers developed AApeptides, a new class of peptidomimetics, to overcome limitations of bioactive peptides. These molecules mimic peptide structure and function, showing promise in biomedical applications.

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Area of Science:

  • Chemical Biology
  • Biomedical Sciences
  • Molecular Probes
  • Drug Discovery

Background:

  • Bioactive peptides face intrinsic limitations in chemical biology and biomedical applications.
  • Research focuses on developing sequence-specific peptidomimetics to mimic peptide and protein structure/function.
  • Modifications in peptide backbone/side chains aim to create biomimetic probes or drug leads.

Purpose of the Study:

  • To expand the family of oligomeric peptidomimetics for broader applications.
  • To introduce a novel class of peptidomimetics, AApeptides, based on a chiral peptide nucleic acid backbone.
  • To highlight the structural design and functions of AApeptides.

Main Methods:

  • Development of AApeptides utilizing a chiral peptide nucleic acid backbone.
  • Exploration of backbone and/or side chain modifications for biomimetic properties.
  • Assessment of AApeptide resistance to proteolytic degradation and chemical diversification.

Main Results:

  • AApeptides demonstrate resistance to proteolytic degradation.
  • AApeptides are amenable to extensive chemical diversification.
  • AApeptides can mimic primary peptide structures and fold into secondary structures like helices and turn-like structures.
  • AApeptides show emerging promise in material and biomedical sciences.

Conclusions:

  • AApeptides represent a promising new class of peptidomimetics with significant potential.
  • Their stability, versatility, and biomimetic capabilities position them for diverse applications.
  • Future development of AApeptides is anticipated to yield advancements in material and biomedical sciences.