A Designed Tryptophan- and Lysine/Arginine-Rich Antimicrobial Peptide with Therapeutic Potential for Clinical Antibiotic-Resistant <i>Candida albicans</i> Vaginitis

New therapeutic agents for <i>Candida albicans</i> vaginitis are urgently awaiting to be developed because of the increasing antibiotic resistance of <i>C. albicans</i>. Antimicrobial peptides (AMPs) are one of the most promising choices for next-generation antibiotics. In this study, novel peptides were designed based on snake venom antimicrobial peptide cathelicidin-BF to promote anti-<i>C. albicans</i> activity and decrease side-effects. The designing strategies include substitutions of charged or hydrophobic amino acid residues for noncharged polar residues to promote antimicrobial activity and insertion of a hydrophobic residue in the hydrophilic side of the helix structure to reduce hemolysis. A designed tryptophan and lysine/arginine-rich cationic peptide <b>4</b> (ZY13) (VKRWKKWR­WKWKKWV-NH₂) exhibited excellent antimicrobial activity against either common strain or clinical isolates of antibiotic-resistant <i>C. albicans</i> with little hemolysis. Peptide <b>4</b> showed significant therapeutic effects on vaginitis in mice induced by the infection of clinical antibiotic-resistant <i>C. albicans</i>. The approaches herein might be useful for designing of AMPs