The self-assembly of a hydrophobic pentapeptide has been investigated in an attempt to develop a drug delivery vehicle. The peptide forms a supramolecular helical column through intra- and intermolecular hydrogen bonding interactions and an interdigitated helical bundle structure in the solid state. In methanol solution, the peptide forms mesoporous vesicles, where the diameters of the vesicles vary with the concentration in direct proportion. The most important property of these mesoporous vesicular structures is the encapsulation of a potent bacteriostatic antibiotic, sulfamethoxazole. Moreover, at pH 6.2, the drug loaded vesicles can effectively release the encapsulated drug slowly, which holds future promise for use of the microvesicles as drug cargo.
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