Self-assembly occurs extensively in biological systems, ranging from cytoskeleton protein filaments in cells to dense plaques of fibrous inappropriately folded protein aggregates in brain tissue.  Although the assemblies share the same nature of peptide and non-covalent interactions, they exhibit drastically different thermal stability.  By mimicking the self-assembly behavior, a class of novel soft material/hydrogel, has been developed for a variety of biomedical applications ranging from 3-D cell cultures and stem cell differentiation to regenerative medicine, controlled drug delivery and tissue engineering.  In previous studies relatively little attention has been paid to the thermodynamic behavior of the assemblies.  For example, temperature dependence of the self-assembly of small molecules is largely unknown.  Here we report on the temperature dependent self-assembly of typical hydrogelators using dynamic light scattering (DLS), NMR, and small angle neutron scattering (SANS).  DLS yields information on the initial stage of fiber formation.  SANS is used to determine the structural characteristics of these supramolecular assemblies (cross-sectional radius of the fibers, average mesh size of the network, etc.).  We believe a better understanding of the self-assembly process will help us to design nanofibers/hydrogels for applications in biology and medicine.

Mechanism of temperature dependent supramolecular fibrillization of small molecules

248th National Meeting (2014)

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