当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF PHARMACEUTICS期刊下所有文献 > Stabilisation and determination of the biological activity of L-asparaginase in poly(D,L-lactide-co-glycolide) nanospheres.

Stabilisation and determination of the biological activity of L-asparaginase in poly(D,L-lactide-co-glycolide) nanospheres.

Abstract：

:The preservation of biological activity of protein drugs in formulations is still a major challenge for successful drug delivery. The enzyme L-asparaginase, which exhibits a short in vivo half-life and is only active against leukaemia in its tetrameric form, was encapsulated in poly(D,L-lactide-co-glycolide) nanospheres by the (w/o)/w-emulsion solvent evaporation technique in presence of various potential stabilisers. Elucidation of the preparation steps revealed that the enzyme is denaturated at the aqueous/organic interface and by sonication. The preparation of L-asparaginase nanospheres with trehalose, PEG 400, and glycerol as components of the inner aqueous phase yielded colloidal formulations with increased biological activity as determined by an improved protocol for quantification of the active enzyme encapsulated. After lyophilisation the enzyme activity and particle size distribution were retained only by use of Pluronic F68 as a lyoprotectant. Despite the unaltered particle size and improved biological activity, the release profile of the enzyme was strongly altered by coencapsulation of the stabilisers resulting in increased first bursts. In consequence, the biological activity of L-asparaginase during preparation and storage can be improved by combining appropriate additives but concurrently the release profile is influenced.

journal_name

Int J Pharm

journal_title

International journal of pharmaceutics

authors

Wolf M,Wirth M,Pittner F,Gabor F

doi

10.1016/s0378-5173(03)00071-1

keywords:

subject

Has Abstract

pub_date

2003-04-30 00:00:00

pages

141-52

issue

1-2

eissn

0378-5173

issn

1873-3476

pii

S0378517303000711

journal_volume

256

pub_type

杂志文章

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