Improvement of StAP3 antimicrobial activity by PEGylation

F.F. MUÑOZ; P.C. CARACCIOLO; G.R. DALEO; G.A. ABRAHAM; M.G. GUEVARA

Potrero de los Funes, San Luis

Simposio; III Escuela Latinoamericana de Nanomedicinas y II Simposio Latinoamericano; 2012

Asociación Argentina de Nanomedicina (Nanomed-ar)

Potato aspartic proteases (StAPs) are proteins with tumoricidal and antimicrobial activities which involve plasma membrane destabilization [1,2]. The StAPs selective cytotoxic activity suggests that these proteins could be used to develop alternative drugs with activity against microbes but not against mammalian cells [3]. On the other hand, PEGylation (i.e. the covalent link of PEG strands) is a technique used to improve pharmaceutical properties of bioactive proteins, mainly improving the serum half-life, and reducing the immunogenicity and the enzymatic degradation [4]. In order to evaluate the ability of PEGylation to improve StAPs antimicrobial activity, we have studied the conjugation of mPEG-SVA (m.w. 5 kDa) to StAP3 under different conditions, and finally compared the cytotoxic activity of StAP3-PEG to that of the native StAP3.