School of Chemistry, Food and Pharmacy, University of Reading, Reading, United Kingdom.
Langmuir. 2012 Aug 21;28(33):12209-15. doi: 10.1021/la302123h. Epub 2012 Aug 6.
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.
我们研究了肽两亲物（PAs），考察了烷基链长对胶原蛋白衍生肽 KTTKS 聚集行为的影响，其应用范围从抗皱美容霜到再生医学的潜在用途。我们研究了合成肽两亲物 C(14)-KTTKS（肉豆蔻酰-Lys-Thr-Thr-Lys-Ser）和 C(18)-KTTKS（硬脂酰-Lys-Thr-Thr-Lys-Ser），以详细研究它们的物理化学性质。据推测，与单独的 KTTKS 相比，这些自组装肽两亲物中的疏水链增强了肽在皮肤中的渗透。随后，C(n)-KTTKS 应该作为前药，通过酶切释放肽。我们的研究结果将有助于具有胶原蛋白刺激活性的分子的进一步开发。
