Self-assembled hydrogel nanoparticle of cholesterol-bearing pullulan as a carrier of protein drugs: complexation and stabilization of insulin
K Akiyoshi, S Kobayashi, S Shichibe, D Mix… - Journal of Controlled …, 1998 - Elsevier
K Akiyoshi, S Kobayashi, S Shichibe, D Mix, M Baudys, SW Kim, J Sunamoto
Journal of Controlled Release, 1998•ElsevierInsulin (Ins) spontaneously and easily complexed with the hydrogel nanoparticle of
hydrophobized cholesterol-bearing pullulan (CHP) in water. The complexed nanoparticles
(diameter 20–30 nm) thus obtained formed a very stable colloid. The thermal denaturation
and subsequent aggregation of Ins were effectively suppressed upon complexation. The
complexed Ins was significantly protected from enzymatic degradation. Spontaneous
dissociation of Ins from the complex was barely observed, except in the presence of bovine …
hydrophobized cholesterol-bearing pullulan (CHP) in water. The complexed nanoparticles
(diameter 20–30 nm) thus obtained formed a very stable colloid. The thermal denaturation
and subsequent aggregation of Ins were effectively suppressed upon complexation. The
complexed Ins was significantly protected from enzymatic degradation. Spontaneous
dissociation of Ins from the complex was barely observed, except in the presence of bovine …
Insulin (Ins) spontaneously and easily complexed with the hydrogel nanoparticle of hydrophobized cholesterol-bearing pullulan (CHP) in water. The complexed nanoparticles (diameter 20–30 nm) thus obtained formed a very stable colloid. The thermal denaturation and subsequent aggregation of Ins were effectively suppressed upon complexation. The complexed Ins was significantly protected from enzymatic degradation. Spontaneous dissociation of Ins from the complex was barely observed, except in the presence of bovine serum albumin. The original physiological activity of complexed Ins was preserved in vivo after i.v. injection.
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