Structural characteristics of short peptides in solution

Protein Pept Lett. 2013 Dec;20(12):1308-23. doi: 10.2174/092986652012131112121417.

Abstract

Short peptides are important biopharmaceuticals as agonistic or antagonistic ligands, aggregation inhibitors, and vaccines, as well as in many other applications. They behave differently from globular proteins in solution. Many short peptides are unstructured and tend to aggregate and undergo structural transition in response to changes in solvent environment, including pH, temperature, ionic strength, presence of organic solvents or surfactants, and exposure to lipid membranes. Such structural transitions are often associated with fibril or β-amyloid formation. These structural characteristics of short peptides have drastic impact on their function, immunogenicity, and storage stability.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry
  • Amyloid / metabolism
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Pliability
  • Protein Conformation
  • Protein Stability*
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / metabolism*

Substances

  • Amyloid
  • Peptides
  • Recombinant Proteins