Conformation and Self-Association of Peptide Amphiphiles Based on the KTTKS Collagen Sequence | Zendy

Pasquale Palladino | Zendy; Valeria Castelletto | Zendy; Ashkan Dehsorkhi | Zendy; Dmitry A. Stetsenko | Zendy; Ian W. Hamley | Zendy

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Conformation and Self-Association of Peptide Amphiphiles Based on the KTTKS Collagen Sequence

Author(s) -

Pasquale Palladino,

Valeria Castelletto,

Ashkan Dehsorkhi,

Dmitry A. Stetsenko,

Ian W. Hamley

Publication year - 2012

Publication title -

langmuir

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.042

H-Index - 333

eISSN - 1520-5827

pISSN - 0743-7463

DOI - 10.1021/la302123h

Subject(s) - amphiphile , peptide , sequence (biology) , chemistry , peptide sequence , association (psychology) , stereochemistry , crystallography , biophysics , biochemistry , biology , organic chemistry , polymer , gene , philosophy , copolymer , epistemology

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.

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