title: Conformation and self-association of peptide amphiphiles based on the KTTKS collagen sequence.
abstract: Studying peptide amphiphiles (PAs), we investigate the influence of alkyl chain length on the aggregation behavior of the collagen-derived peptide KTTKS with applications ranging from antiwrinkle cosmetic creams to potential uses in regenerative medicine. We have studied synthetic peptides amphiphiles C(14)-KTTKS (myristoyl-Lys-Thr-Thr-Lys-Ser) and C(18)-KTTKS (stearoyl-Lys-Thr-Thr-Lys-Ser) to investigate in detail their physicochemical properties. It is presumed that the hydrophobic chain in these self-assembling peptide amphiphiles enhances peptide permeation across the skin compared to KTTKS alone. Subsequently C(n)-KTTKS should act as a prodrug and release the peptide by enzymatic cleavage. Our results should be useful in the further development of molecules with collagen-stimulating activity.
authors: School of Chemistry, Food and Pharmacy, University of Reading, Reading, United Kingdom.
authors: Pasquale
authors: P
authors: Palladino
authors: Valeria
authors: V
authors: Castelletto
authors: Ashkan
authors: A
authors: Dehsorkhi
authors: Dmitry
authors: D
authors: Stetsenko
authors: Ian W
authors: IW
authors: Hamley
mesh_terms: D003094:Collagen / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D010539:Permeability; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D012867:Skin / Q000378:metabolism
chemical_list: D009842:Oligopeptides; D010446:Peptide Fragments; D003094:Collagen