SYNTHESIS OF DIPEPTIDES AND I N V I T R O EVALUATION OF ANTIFUNGAL ACTIVITY

N-Tert-butoxycarbonylglycyl-(S)-β-imidazolyl-α-alanine and N-tert-butoxycarbonylglycyl-(S)-[4-allyl-3-(3'-hydroxypropyl)-5-thioxo-1,2,4-triazol-1-yl]-α-alanine dipeptides, previously not described in the literature, were synthesized using the activated ester method for classical peptide synthesis. The structures of these synthesized dipeptides were confirmed through NMR spectroscopic analysis. The antifungal activity of initial non-protein amino acids and synthesized dipeptides was studied by choosing wide spread pathogenic and conditionally pathogenic fungal strains as test fungi: Aspergillus versicolor 12134, A. flavus 10567, A. candidus 10711, Penicillium chrysogenum 8190, P. aurantiogriseum 12053, P. funiculosum 8258, Alternaria alternata 8126, Ulocladium botrytis 12027, Aureobasidium pullulans 8269. The antifungal activity of the initial (S)-β-imidazolyl-α-alanine amino acid is notable against the P. aurantiogriseum 12053 and U. botrytis 12027 fungal strains. N-Tert-butoxycarbonylglycyl-(S)-β-imidazolyl-α-alanine dipeptide demonstrates a strong inhibitory effect specifically on the P. aurantiogriseum 12053 strain, with a similar level of inhibition observed at a concentration of 0.6 mL (0.331 mmol/mL). The initial amino acid exhibited comparable inhibition at a higher volume of 0.9 mL (0.495 mmol/mL). In contrast, the (S)-[4-allyl-3-(3'-hydroxypropyl)-5-thioxo-1,2,4-triazol-1-yl]-α-alaninе amino acid effectively suppresses the growth of multiple strains, including P. aurantiogriseum 12053, P. funiculosum 8258, U. botrytis 12027, and A. pullulans 8269, when tested at 0.9 mL (0.495 mmol/mL). The corresponding N-tert-butoxycarbonylglycyl-(S)-[4-allyl-3-(3'-hydroxypropyl)-5-thioxo-1,2,4-triazol-1-yl]-α-alanine dipeptide also shows significant inhibitory effects similar to those of (S)-[4-allyl-3-(3'-hydroxypropyl)-5-thioxo-1,2,4-triazol-1-yl]-α-alaninе.