Human insulin versus porcine insulin in rhesus monkeys with diabetes mellitus

Jin, Xi; Zeng, Li; Zhang, Shuang; He, Sirong; Ren, Yan; Chen, Younan; Wei, Lingling; Wang, Li; Li, Hongxia; Cheng, Jun; Liu, Yanrong

doi:10.1111/jmp.12025

Cited by 2 publications

(1 citation statement)

References 22 publications

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“…Insulin, a protein secreted by the β cells of the pancreas, is one of the most important therapeutic agents for insulin-dependent (type I) and deteriorative insulin-independent (type II) diabetes mellitus [4], and commonly administered subcutaneously; however, besides pain, which may bring about unwanted complications, e.g. allergic reactions, hyperinsulinemia, insulin lipodystrophy around the injection site [5]. Problems encountered with insulin injection vitalize the demands to develop alternative delivery systems.…”

Section: Introductionmentioning

confidence: 99%

Enhanced hypoglycemic effect of biotin-modified liposomes loading insulin: effect of formulation variables, intracellular trafficking, and cytotoxicity

Zhang

Lü

et al. 2014

Nanoscale Res Lett

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Peroral protein/peptide delivery has been one of the most challenging, but encouraging topics in pharmaceutics. This article was intended to explore the potential of biotin-modified liposomes (BLPs) as oral insulin delivery carriers. By incorporating biotin-DSPE into the lipid bilayer, we prepared BLPs using reverse evaporation/sonication method. We investigated hypoglycemic effects in normal rats after oral administration of BLPs, and the possible absorption mechanism by a series of in vitro tests. The relative pharmacological bioavailability of BLPs was up to 11.04% that was as much as 5.28 folds of conventional liposomes (CLPs). The results showed that the enhanced oral absorption of insulin mainly attributed to biotin ligand-mediated endocytosis. The results provided proof of BLPs as effective carriers for oral insulin delivery.

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Section: Introductionmentioning

confidence: 99%

Enhanced hypoglycemic effect of biotin-modified liposomes loading insulin: effect of formulation variables, intracellular trafficking, and cytotoxicity

Zhang

Lü

et al. 2014

Nanoscale Res Lett

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A molecular simulation study of the protection of insulin bioactive structure by trehalose

Liu

et al. 2014

J Mol Model

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Biopharmaceuticals are proteins with a crucial role in the treatment of many diseases. However, these protein medicines are often thermally labile and therefore unsuitable for long-term application and storage, as they tend to lose their activity under ambient conditions. Desiccation is one approach to improving protein stability, but the drying process itself can cause irreversible damage. In the current study, insulin was chosen as an example of a thermally sensitive biopharmaceutical to investigate whether the disaccharide, trehalose, can prevent loss of structural integrity due to drying. The experiment was performed using replica exchange molecular simulation and Gromacs software with a Gromos96 (53a6) force field. The results indicate that trehalose preserves the bioactive structure of insulin during drying, consistent with the use of trehalose as a protectant for thermally sensitive biopharmaceuticals. For instance, at the water content of 1.77%, insulin without any protectants yields the highest RMSD value as 0.451 nm, then the RMSD of insulin in presence of trehalose only ca. 0.100 nm.

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Human insulin versus porcine insulin in rhesus monkeys with diabetes mellitus

Abstract: Porcine insulin as a competent candidate for regular insulin therapy to maintain blood glucose levels in insulin-dependent diabetic monkeys during preclinical studies of islet transplantation.

Cited by 2 publications

References 22 publications

Enhanced hypoglycemic effect of biotin-modified liposomes loading insulin: effect of formulation variables, intracellular trafficking, and cytotoxicity

Enhanced hypoglycemic effect of biotin-modified liposomes loading insulin: effect of formulation variables, intracellular trafficking, and cytotoxicity

A molecular simulation study of the protection of insulin bioactive structure by trehalose

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