Structural Characteristics of Short Peptides in Solution

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.

Cite this article as:

Ohtake Satoshi, Kita Yoshiko, Payne Robert, Manning Mark and Arakawa Tsutomu, Structural Characteristics of Short Peptides in Solution, Protein & Peptide Letters 2013; 20 (12) . https://dx.doi.org/10.2174/092986652012131112121417