Spin coating mediated morphology modulation in self assembly of peptides

Controlling the morphology and nanostructure of self-assembled peptide molecules is of fundamental importance to chemistry and material science due to their bioactivity in both in vivo and in vitro settings, ability to act as templates for conjugating bio-recognition elements, hybrid supramolecular assembly, possible detection and treatment of diseases and so on. In this article, we show that spin coating, a widely utilized method for obtaining ultra-thin polymer films, has been utilised to modulate the self-assembly of peptide molecules, which has traditionally been achieved by chemical functionalisation of the molecules. With the specific example of diphenylalanine-based peptide molecules, we show that a variety of self-assembled architectures such as long fibrils, short fibrils, globules, nanodots, and so on, spanning over large areas can be obtained by simultaneously varying the spinning speed (RPM) and the solution concentration (C-p) during spin coating. We correlate the variation in morphology to a transition from spin dewetting at very low C-p (or high RPM) to the formation of continuous films at high C-p (or low RPM) during the initial stage of spin coating. We further show the generality of the approach by achieving distinct self-assembled morphologies with diphenylalanine analogues with different C-terminal and N-terminal groups by modulation of spin coating parameters, though the exact morphology obtained under identical coating conditions depends on the chemical nature of the peptide molecules. The work opens up a new possible route for creating complex peptide assemblies on demand by simultaneous control of molecular functionalisation and spin coating parameters vis - a - vis the applied centrifugal force.

Automated summary

This article discusses the control of self-assembled peptide molecules' morphology and nanostructure using spin coating. By adjusting spin coating parameters, different morphologies of self-assembled structures can be obtained. This method opens up a new potential route for creating complex peptide assemblies on demand.