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

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• 作者：Pasquale Palladino ; Valeria Castelletto ; Ashkan Dehsorkhi ; Dmitry Stetsenko ; Ian W. Hamley
• 刊名：Langmuir
• 出版年：2012
• 出版时间：August 21, 2012
• 年：2012
• 卷：28
• 期：33
• 页码：12209-12215
• 全文大小：425K
• 年卷期：v.28,no.33(August 21, 2012)
• ISSN：1520-5827

文摘

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鈥揔TTKS (myristoyl-Lys-Thr-Thr-Lys-Ser) and C₁₈鈥揔TTKS (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_<i>ni>鈥揔TTKS 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.