Alteration of the Antifungal Action Mechanism Due to Structural Changes in the Antimicrobial Peptide, HnMc
Source abstract
Abstract
The rapid induction of drug resistance is considered a fatal drawback of conventional antibiotics and requires the continuous development of new antibiotics. Accordingly, antibacterial peptides (AMPs) have attracted interest as next-generation antibiotics and many studies have been conducted. However, much remains unknown regarding the mechanism of AMPs and the effects of amino acid sequence changes. We compared the structures and antifungal effects of HnMc-W (F1W substitution, straight alpha-helical structure), HnMc-WP1 (S9P substitution, bending alpha-helical structure), and HnMc-WP2 (addition of the PXXP motif, helix-to-helix structure) to those of a parent hybrid AMP (HnMc) regarding their mechanism of action. The most active was HnMc-WP2, which exhibited an antifungal effect via membranolytic action on the fungal cell membrane. The others inhibited fungal growth by inducing apoptosis through reactive oxygen species production caused by mitochondrial damage. This study proposes the addition of the ‘PXXP’ motif in the design of AMPs acting on cell membranes.
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Research context
OpenAlex topics: Antimicrobial Peptides and Activities · Insect and Pesticide Research · Polydiacetylene-based materials and applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Laboratory Medicine, Inje University Haeundae Paik Hospital, Busan 48108, Republic of Korea
Master of Technical Sciences in Clinical Laboratory Science, Daejeon Health University, Daejeon 34504, Republic of Korea
Department of Clinical Laboratory Science, Daejeon Health University, Daejeon 34504, Republic of Korea
Department of Chemical Engineering, Sunchon National University, Suncheon 57922, Republic of Korea
Funding
Meister Support Project of DAEJEON HEALTH UNIVERSITY
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