Evaluation of in vitro cytotoxic activity of mono-PEGylated StAP3 (Solanum tuberosum Aspartic Protease 3) forms

FERNANDO MUÑOZ; PABLO CARACCIOLO; GUSTAVO R. DALEO,; GUSTAVO ABRAHAM; MARÍA G. GUEVARA.

Biotechnology Reports

Elsevier B.V.

Lugar: Amsterdam; Año: 2014 vol. 3 p. 1 - 7

2215-017X

tStAP3 is a plant aspartic protease with cytotoxic activity toward a broad spectrum of pathogens, includingpotato and human pathogen microorganisms, and cancer cells, but not against human T cells, human redblood cells or plant cells. For this reason, StAP3 could be a promising and potential drug candidate forfuture therapies. In this work, the improvement of the performance of StAP3 was achieved by meansof a modification with PEG. The separation of a mono-PEGylated StAP3 fraction was easily performedby gel filtration chromatography. The mono-PEGylated StAP3 fraction was studied in terms of in vitroantimicrobial activity, exhibiting higher antimicrobial activity against Fusarium solani spores and Bacilluscereus, but slightly lower activity against Escherichia coli than native protein. Such increase in antifungalactivity has not been reported previously for a PEGylated plant protein. In addition, PEGylation did notaffect the selective cytotoxicity of StAP3, since no hemolytic activity was observed.