Degradability of poly(L-lysine) and poly(DL-aminoserinate) complexed with a polyanion under conditions modelling physico-chemical characteristics of body fluids

Poly(L-lysine), (PLL), and poly(DL-amino serinate), (PSA), are respectively enzymatically and hydrolytically degradable polycations. This work was aimed at investigating their degradability when they are complexed with polyanions, namely poly(acrylic acid) and poly(L-lysine citramide), taken as simp...

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Bibliographic Details
Published in:Journal of colloid and interface science 2010, Vol.350, p.459-464
Main Authors: Leclercq, Laurent, Boustta, Mahfoud, Rixte, Johan, Vert, Michel
Format: Article
Language:English
Subjects:
Chemical Sciences
Organic chemistry
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Summary:Poly(L-lysine), (PLL), and poly(DL-amino serinate), (PSA), are respectively enzymatically and hydrolytically degradable polycations. This work was aimed at investigating their degradability when they are complexed with polyanions, namely poly(acrylic acid) and poly(L-lysine citramide), taken as simple models of DNA in polyplexes. Comparison was made with degradation characteristics of the same polycations in solution in the absence of polyanion on the basis of size exclusion chromatography and capillary zone electrophoresis. Complexed PLL remained enzymatically degradable by trypsin, an endopeptidase, but was no longer degradable by aminopeptidase, an exopeptidase. Trypsin yielded a mixture of trilysin and tetralysin. Complexed PSA remained hydrolytically degradable in aqueous media. The hydrolysis of PSA led to DL-serine. However, traces of anionic species were also detected that were identified as residues of constituting repeating units issued from the N-benzyloxycarbonyl polyaminoserinate precursor (PSAZ).
ISSN:0021-9797
1095-7103
DOI:10.1016/j.cis.2010.07.015