Drug Discov Ther. 2009;3(5):208-214.

Structure analysis of short peptides by analytical ultracentrifugation: Review.

Arakawa T, Niikura T, Kita Y, Arisaka F


Short peptides are potential drug candidates for pharmaceutical and biotech industries. Short peptides are natural ligands for numerous G-protein coupled receptors (GPCR) and hence constitute a large number of drug candidates. Synthetic short peptides are also extensively developed as agonistic or antagonistic ligands that function in a similar manner to antibodies, soluble receptors and protein ligands. Characterization of the peptides in solution is often performed in the presence of organic solvents, which can presumably generate the structure bound to the target surface and also enhance the solubility of the peptides. Analytical ultracentrifugation (AUC) technique should provide information on the state of self-association of the peptide in solution. Its application for short peptides has been far less than the applications for proteins. We believe that AUC should be used to show the associated state of the peptides, as reviewed in this paper.

KEYWORDS: Analytical ultracentrifugation, sedimentation, peptide, aggregation, disordered structure

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