Structure and Function in Peptide-based Supramolecular Designs

Released on by William Seth Horne
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  • Structure and Function in Peptide-based Supramolecular Designs Book Detail

  • Author : William Seth Horne
  • Release Date : 2005
  • Publisher :
  • Genre : Cyclic peptides
  • Pages : 456
  • ISBN 13 :
  • File Size : 76,76 MB
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Structure and Function in Peptide-based Supramolecular Designs by William Seth Horne PDF Summary

Book Description: Chemical synthesis of peptides grants the ability to expand beyond amino acid side chains found in nature as well as the connectivity of the peptide backbone. These synthetic modifications can control peptide structure and properties as well as create new methods for the preparation of biologically inspired structures. In the course of the research presented, the structural and functional consequences of synthetic peptide modifications are explored in several systems. In a project examining structural effects of chemical modifications to the peptide backbone, a variety of peptides incorporating 1,4-disubstituted-1,2,3-triazole [epsilon]-amino acids are described. Effects of triazole backbone modifications in designed cyclic structures as well as protein-like linear architectures are examined. In an effort to expand on the known capacity of cyclic D,L-[alpha]-peptides to disrupt biological membranes, sequences capable of inhibiting virus infection of mammalian cells are examined. A compound that inhibits adenovirus infection of host cells at [micro]M doses through disruption of an endosomal pH gradient key in the infection cycle of a number of viral pathogens is described. In a project aimed toward fabrication of conductive materials from self-assembling peptides, cyclic D,L-[alpha]-bearing side chains introduced to modify electronic properties in an assembled nanotubular architecture are discussed. It is demonstrated that the hydrogen bond directed self-assembly of the cyclic D,L-[alpha]-peptide backbone can promote charge transfer between aromatic side chains and that peptide self-association can be controlled through electrochemical charge state of redox-active side chains. In total, the work summarized in this thesis builds on the idea of peptides and proteins as scaffolds for the design of supramolecular assemblies with interesting structural and functional properties.

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