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Peptide Bonds02:43

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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 chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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The mechanism for anionic chain-growth polymerization involves initiation, propagation, and termination steps. In the initiation step, a nucleophilic anion, such as butyl lithium, initiates the polymerization process by attacking the π bond of the vinylic monomer. As a result, a carbanion, stabilized by the electron‐withdrawing group, is generated. The resulting carbanion acts as a Michael donor in the propagation step and attacks the second vinylic monomer, which acts as a Michael...
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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Effects of Cyclization on Peptide Backbone Dynamics.

Conan K Wang1, Joakim E Swedberg1, Susan E Northfield1

  • 1Institute for Molecular Bioscience, The University of Queensland , Brisbane, Queensland 4072, Australia.

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|December 4, 2015
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Peptide cyclization impacts internal dynamics differently. Disulfide bonds enhance rigidity more than backbone cyclization, especially in complex polycyclic peptides, revealing a complex interplay.

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Area of Science:

  • Biophysical Chemistry
  • Peptide Science
  • Structural Biology

Background:

  • Cyclization is a key strategy for peptide structure optimization in drug development.
  • The influence of different cyclization methods on peptide internal dynamics remains poorly understood.
  • Understanding these dynamics is crucial for designing peptides with improved biopharmaceutical properties.

Purpose of the Study:

  • To investigate the effects of backbone and disulfide-bond cyclization on peptide internal dynamics.
  • To compare the rigidity contributions of macrocyclization versus internal cyclization in peptides.
  • To elucidate the relationship between cyclization strategies and the conformational flexibility of peptides.

Main Methods:

  • Employed multifield Nuclear Magnetic Resonance (NMR) relaxation measurements.
  • Utilized molecular dynamics (MD) simulations.
  • Studied model peptides: monocyclic VH, bicyclic SFTI-1, and polycyclic cVc1.1, alongside linear analogues.

Main Results:

  • Backbone cyclization increased rigidity in the monocyclic peptide VH.
  • In bicyclic SFTI-1, backbone cyclization had minimal impact on rigidity; disulfide bonds showed an 'insulating' effect.
  • Disulfide bonds contributed more significantly to overall peptide rigidity than backbone macrocyclization.

Conclusions:

  • Backbone cyclization can enhance peptide rigidity, but its effect is context-dependent.
  • Disulfide bonds offer a substantial rigidity contribution and can insulate internal peptide structures.
  • The interplay between cyclization type and peptide architecture dictates the resulting internal dynamics and rigidity.