Abstract

Antimicrobial peptides are short peptides (< 100 amino acids) that have a potent function against microbial invasion. These peptides are produced by various organisms, including bacteria, fungi, flowering and non-flowering plants, insects and mammals. Antifungal peptides are a major group of antimicrobial peptides that have a specially potent effect against fungi. Several parameters affect the activity of antifungal peptides, including the sequence, size, charge, degree of structure formation, cationicity, hydrophobicity and amphipathicity. By analysis of numerous antifungal peptide sequences, the roles of these parameters in the structure of antifungal peptides are investigated in this review and by the in silico analysis of the existing residues, occupying each position of sequence, a template sequence is defined to generate potent and efficient lead antifungal peptides.

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