Conformation and self-association of peptide amphiphiles based on the KTTKS collagen sequence
Palladino, P., Castelletto, V., Dehsorkhi, A., Stetsenko, D. and Hamley, I. W. (2012) Conformation and self-association of peptide amphiphiles based on the KTTKS collagen sequence. Langmuir, 28 (33). pp. 12209-12215. ISSN 0743-7463
To link to this article DOI: 10.1021/la302123h
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 C14− KTTKS (myristoyl Lys-Thr-Thr-Lys-Ser) and C18−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 Cn−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.