title: Structural characteristics of short peptides in solution.
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.
authors.affiliation: Pfizer, 700 Chesterfield Parkway West, Chesterfield, MO 63017, USA. satoshi.ohtake@pfizer.com.
authors.forename: Satoshi
authors.initials: S
authors.lastname: Ohtake
authors.forename: Yoshiko
authors.initials: Y
authors.lastname: Kita
authors.forename: Robert
authors.initials: R
authors.lastname: Payne
authors.forename: Mark
authors.initials: M
authors.lastname: Manning
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Arakawa
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D018583:Pliability; D011487:Protein Conformation; D055550:Protein Stability; D011994:Recombinant Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000682:Amyloid; D010455:Peptides; D011994:Recombinant Proteins