RESUMEN
The self-assembly of three cosmetically active peptide amphiphiles C16-GHK, C16-KT, and C16-KTTKS (C16 denotes a hexadecyl, palmitoyl chain) used in commercial skin care products is examined. A range of spectroscopic, microscopic, and X-ray scattering methods is used to probe the secondary structure, aggregate morphology, and the nanostructure. Peptide amphiphile (PA) C16-KTTKS forms flat tapes and extended fibrillar structures with high ß-sheet content. In contrast, C16-KT and C16-GHK exhibit crystal-like aggregates with, in the case of the latter PA, lower ß-sheet content. All three PA samples show spacings from bilayer structures in small-angle X-ray scattering profiles, and all three have similar critical aggregation concentrations, this being governed by the lipid chain length. However, only C16-KTTKS is stained by Congo red, a diagnostic dye used to detect amyloid formation, and this PA also shows a highly aligned cross-ß X-ray diffraction pattern consistent with the high ß-sheet content in the self-assembled aggregates. These findings may provide important insights relevant to the role of self-assembled aggregates on the reported collagen-stimulating properties of these PAs.
Asunto(s)
Cosméticos/química , Lipopéptidos/química , Ácido Palmítico/química , Cuidados de la Piel , Secuencia de Aminoácidos , Interacciones Hidrofóbicas e HidrofílicasRESUMEN
A novel concept of a membrane-based micro-array biosensor is presented. The methodology is based on a single lipid membrane interrogated with electrochemical impedance techniques followed by multivariate data analysis. A single membrane is designed so that relaxation processes with a range of time constants can be probed at different potentials. A range of other approaches cited in the literature is reviewed.