Substrate specificity of peptide permeases in Candida albicans Free

Specificity of peptide transport systems in Candida albicans was studied using as an experimental tool novel anticandidal peptides, containing the N³-4-methoxyfumaroyl-l-2,3-diamino-propanoic acid residue. Studies on cross-resistance and on peptide uptake by spontaneous mutants resistant to toxic peptides, confirmed the multiplicity of peptide permeases in Candida albicans. At least two peptide permeases exist in this microorganism; the first one, specific for di- and tripeptides and the second, for oligopeptides containing 3–6 amino acids. The rate of the tritetra tetra-, penta- and hexapeptide transport in the mycelial form of Candida albicans is about 2-times higher than in the yeast form, while that of dipeptides is markedly reduced.

Tripeptides are proposed as the most efficient carriers for the delivery of ‘warhead’ amino acids into Candida albicans cells.