Abstract
AbstractThe self‐assembly features of a family of tetrapeptides with a silk‐inspired structure are presented. An exhaustive study of the influence of the terminal alkyl chain length in this process is undertaken. Scanning electron microscopy (SEM), wide‐angle X‐ray diffraction (WAXD), FTIR spectroscopy, and circular dichroism were used for structural analysis. These compounds, as in the natural model, self‐assemble into antiparallel β‐sheet structures that further organize to form fibrillar aggregates. Furthermore, some of them arecapable of forming a crowded network that entraps thesolvent leading to physical gels with different microscopic morphologies. A model for the assembly process is proposed.(© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)
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