Micelle-like Nanoassemblies of Short Peptides Create Antimicrobial Selectivity in a Conventional Antifungal Drug

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TABLE OF CONTENTS

Novel antifungal selectivity was created in a conventional antifungal drug, amphotericin B (AmB)

via the co-assembly formation with a short-peptide hydrogelator (P1). The co-assembly complex

suppressed the intrinsic antifungal activity. When P1 in the complex was degraded by a protease

secreted from a fungus, the suppressed antifungal activity of AmB recovered, resulting in the

selective killing of the fungus.

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