Title:Structural Characteristics of Short Peptides in Solution
Volume: 20
Issue: 12
Author(s): Satoshi Ohtake, Yoshiko Kita, Robert Payne, Mark Manning and Tsutomu Arakawa
Affiliation:
Keywords:
Peptide, structure flexibility, membrane, aggregation, formulation, vaccine.
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.
