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M Nuruzzaman Khan1 Yutaka Kuwahara1 Makoto Takafuji1 Hirotaka Ihara1

1, Kumamoto University, Kumamoto, , Japan

Herein, we present a simple and versatile method for morphological enhanced stabilization and transcription of beta-lactoglobulin (ßlg). This globular protein spontaneously self-assemble to soluble spherical aggregate (ca. 80-300 nm) upon heat treatment at definite pH. Our approach involves the construction of π-conjugated co-polymer coating around the outer surface of protein spheres. Here we used for the first time, 1,5-dihydroxynapthalene and 1,3,5-trimethyl-1,3,5-triazinane for surface modification of ßlg amphiphilic protein, which crosslinked on the protein surface with extension of π-conjugated structures by in situ co-polymerization at room temperature (298 K). Further the obtained core-shell structure composed of π-conjugated polymer-coated ßlg protein sphere was transformed to hollow carbon nanosphere with tailored properties by carbonization at high temperature. The hollow spheres were characterized by using transmission electron microscopy (TEM). The cross sectional analysis with field emission scanning electron microscopy (FE SEM) of core-shell structure revealed polymer coating on the ßlg protein surface. The obtained conjugated polymer and carbon hollow sphere were further characterized by energy dispersive x-ray spectroscopy (EDS), solid state NMR, dynamic light scattering (DLS). The surface properties of prepared organic and carbon nanosphere can be adjusted by hybridization of different types of functional materials and provides interesting platform for nanoarchitectonics.

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