A preference for several amino acids is observed to occur at particular positions of cationic α‐helical antimicrobial peptides (AMPs), which ensures the formation of amphipathic regions once they assume their correct secondary structure in membranes or membrane‐mimicking environments and makes them active against pathogens. This study determined the effect of alanine mutations on the secondary structure and bioactivity of lyp1987 (GRLQAFLAKMKEIAAQTL‐NH 2 ), a cationic α‐helical AMP obtained from the venom of Lycosa poonaensis which exhibits broad range activity against Gram‐positive and Gram‐negative bacteria with micromolar minimum inhibitory concentrations (MIC). CD spectroscopy revealed no significant difference in the secondary structure, with all alanine‐substituted analogs exhibiting predominantly α‐helical structure in buffered 2,2,2‐trifluoroethanol solution. Alanine substitution at Glu12 and Thr17 increased the activity of lyp1987 against Gram‐positive and ‐negative bacteria, while alanine substitution at Lys9 increased its selectivity against Gram‐positive bacteria. Further investigation can be done to determine positions and substitutions that will give less cytotoxic analogs.
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Fernando et al. (2024) studied this question.
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