Structural Characteristics of Short Peptides in Solution

Author(s): Satoshi Ohtake, Yoshiko Kita, Robert Payne, Mark Manning, Tsutomu Arakawa

Journal Name: Protein & Peptide Letters

Volume 20 , Issue 12 , 2013

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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.

Keywords: Peptide, structure flexibility, membrane, aggregation, formulation, vaccine.

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Article Details

Year: 2013
Page: [1308 - 1323]
Pages: 16
DOI: 10.2174/092986652012131112121417
Price: $65

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