Muñoz Fernando, Caracciolo Pablo C, Daleo Gustavo, Abraham Gustavo A, Guevara M Gabriela
Plant Biochemistry Laboratory, Biological Research Institute, IIB (UNMdP-CONICET), Funes 3250, 7600, Mar del Plata, Argentina.
Instituto de Investigaciones en Ciencia y Tecnología de Materiales, INTEMA (UNMdP-CONICET), Av. Juan B. Justo 4302, 7600, Mar del Plata, Argentina.
Biotechnol Rep (Amst). 2014 May 27;3:1-7. doi: 10.1016/j.btre.2014.05.007. eCollection 2014 Sep.
AP3 is a plant aspartic protease with cytotoxic activity toward a broad spectrum of pathogens, including potato and human pathogen microorganisms, and cancer cells, but not against human T cells, human red blood cells or plant cells. For this reason, AP3 could be a promising and potential drug candidate for future therapies. In this work, the improvement of the performance of AP3 was achieved by means of a modification with PEG. The separation of a mono-PEGylated AP3 fraction was easily performed by gel filtration chromatography. The mono-PEGylated AP3 fraction was studied in terms of antimicrobial activity, exhibiting higher antimicrobial activity against spores and , but slightly lower activity against than native protein. Such increase in antifungal activity has not been reported previously for a PEGylated plant protein. In addition, PEGylation did not affect the selective cytotoxicity of AP3, since no hemolytic activity was observed.
AP3是一种植物天冬氨酸蛋白酶，对包括马铃薯和人类致病微生物以及癌细胞在内的多种病原体具有细胞毒性活性，但对人类T细胞、人类红细胞或植物细胞无毒性。因此，AP3可能是未来治疗中一种有前景的潜在药物候选物。在这项工作中，通过用聚乙二醇（PEG）修饰实现了AP3性能的改善。通过凝胶过滤色谱法很容易分离出单聚乙二醇化AP3组分。对单聚乙二醇化AP3组分的抗菌活性进行了研究，结果表明其对孢子具有更高的抗菌活性，对[此处原文缺失相关内容]的活性略低于天然蛋白。此前尚未有关于聚乙二醇化植物蛋白抗真菌活性增加的报道。此外，聚乙二醇化不影响AP3的选择性细胞毒性，因为未观察到溶血活性。
