The antifungal activity of GIK-modified amphiphilic peptides

The fungal infection has emerged as a significant global health concern primarily due to the misuse of drugs resulting from multidrug resistance and the slow pace of developing new antifungal agents. However, antifungal peptides (AFPs) may be a competitive candidate for solving this dilemma. AFPs function by binding to fungal membranes via surface electrostatic potentials, subsequently inducing membrane depolarization and increased permeability through hydrophobic interactions. This mechanism acts swiftly, effectively eliminating pathogens before resistance mechanisms can develop. Compared to natural AFPs, synthetic AFPs display enhanced properties including low toxicity to host cells, fewer unknown side effects, sufficient efficacy, stability, simpler sequences and low production costs and GIK with the sequence G(IIKK)3I-NH2 is spurious among them as an antifungal agent. Modifying GIK by altering the amino acids sequence to manipulate its electoral and hydrophobic properties may refine this amphophilic peptide's antifungal.