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. ORCID: https://orcid.org/0000-0002-4549-0926 (2012) Conformation and self-association of peptide amphiphiles based on the KTTKS collagen sequence. Langmuir, 28 (33). pp. 12209-12215. ISSN 0743-7463 doi: 10.1021/la302123h

Abstract/Summary

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.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/29286
Identification Number/DOI	10.1021/la302123h
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) > Electron Microscopy Laboratory (CAF)
Publisher	American Chemical Society
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