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Formation of native disulfide bond patterns in small antifungal proteins and their gamma-core optimized analogs

Year: 2024
Type: conference-paper
Abstract: The -cores of the PAF and NFAP2 antifungal proteins were replaced by an optimized peptide sequence, and the modified analogs were synthesized by chemical methods.PAF imp could only be prepared by NCL from two fragments, and oxidation in a GSH-GSSG buffer led to native disulfide connectivity.The PAF imp protein showed stronger inhibitory activity against Candida albicans compared to PAF, proving the role of -core in the antifungal effect.NFAP2 imp was prepared by stepwise solid-phase synthesis, applying orthogonal thiol protection.For this, the native disulfide bond pattern of NFAP2 was determined first, and it was found to be abbcac.The disulfide bridges were formed regioselectively.The produced NFAP2 imp was less effective against Candida albicans than NFAP2, pointing to the importance of the -core in stabilizing the structure and not in the antifungal activity.
DOI: 10.17952/37eps.2024.p1287
Authors: Györgyi Váradi, László Galgóczy, András Czajlik, Attila Borics, Gábor Bende, Csaba Papp, Zoltán Kele, Gyula Batta, Gábor K. Tóth
Language: English
Open Access status: bronze
Awards: G134384773, G2012631447, G3382482514, G3463726684, G3784062111, G7596933463, G7694217703, G7857699461
OpenAlex ID: W4402744714
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