Abstract

This paper presents the construction of hollow peptide microspheres and the mechanism of transition of microspheres to rod-like vesicles at low concentration. The tripeptides Boc-Phe-Maba-Phe-OMe 1 and Boc-Phe-Maba-Tyr-OMe 2, each of them containing a rigid m-aminobenzoic acid (Maba) template at the central position, forms microspheres at a concentration of 1.6 mM in methanol. At low concentration, these vesicular structures are fused through neck formation, and this leads to sphere-to-rod transition of vesicles. Sizes of these microspheres increase with increasing concentration. We have successfully characterized this transition by fluorescence spectroscopy, DLS, and electron microscopic study. The scanning electron microscopy clearly shows that these spheres are hollow. One important property of these microvesicular structures is the encapsulation of a potent anticonvulsant and mood stabilizing drug carbamazepine, which holds future promise to use these microvesicles as delivery vehicles.

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