Elsevier

Biomaterials

Volume 17, Issue 7, 1996, Pages 715-723
Biomaterials

Paper
Degradation of poly(d,l-lactic acid) nanoparticles coated with albumin in model digestive fluids (USP XXII)

https://doi.org/10.1016/0142-9612(96)86742-1Get rights and content

Abstract

Entirely biodegradable poly(d,l-lactic acid) (PLA50) nanoparticles coated with albumin were prepared by the solvent evaporation technique. Their degradative properties were investigated in simulated gastric and intestinal fluids (USP XXII). The degradation of the albumin coating was monitored by HPLC, whereas PLA50 degradation was determined by size exclusion chromatography (SEC) as well as by the detection of lactate in bulk solution by enzymatic assay. As expected, the coating effect of albumin, a readily digestible protein, rapidly disappeared in both gastric and intestinal media, thus exposing albumin-free PLA50 cores to hydrolytic processes. In pepsin-rich simulated gastric fluid, no degradation of the PLA50 core was observed over 8 h incubation time. In contrast, in pancreatin-rich simulated intestinal fluid, the PLA50 nanoparticles were rapidly converted into lactate. The results showed that the PLA50 degradation was mainly due to an enzymatic cleavage process. Further experiments showed the involvement of lipases in the degradation of the PLA50 core in simulated intestinal fluid.

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      Citation Excerpt :

      As expected, due to the important exposure to the enzymes of the oily core of the NE prepared without non-ionic surfactants, this was the formulation that presented the highest degradation by pancreatic enzymes (70% in 20 min), being its area under the curve significantly higher than those corresponding to CS NCs (p ≤ 0.0001) and PARG NCs (p ≤ 0.001). This was mainly attributed to the interaction of the pancreatic lipase with the oily droplets [19,60,68], being this degradation slightly reduced by the CS and PARG coatings. We have speculated that this limited protective effect of the polymeric shell could be attributed to the presence of amylases, enzymes with the capacity of degrading CS through the α(1,4) glycosidic bond cleavage [69–71], and peptidases, enzymes capable of degrading PARG backbone through the peptide bond [68,72].

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