Insulin aspart: a novel rapid-acting human insulin analogue
- 1 September 1999
- journal article
- Published by Informa Healthcare in Expert Opinion on Investigational Drugs
- Vol. 8 (9) , 1431-1442
- https://doi.org/10.1517/13543784.8.9.1431
Abstract
In order to improve therapy and increase the quality of life for diabetic patients, it has been of significant interest to develop rapid-acting insulin preparations that mimic the physiological meal-time profile of insulin more closely than soluble human insulin. Insulin aspart (B28Asp human insulin) is a novel rapid-acting insulin analogue that fulfils this criterion. The B28Asp modification weakens the self-association of the insulin molecule and provides a more rapid absorption from the sc. injection site. The preclinical evaluation in vitro and in vivo demonstrates that apart from the more rapid absorption, insulin aspart is equivalent to human insulin. Thus, insulin aspart is equivalent to human insulin on key in vitro parameters such as insulin receptor affinity, insulin receptor dissociation rate, insulin receptor tyrosine kinase activation, IGF-I receptor binding affinity, metabolic and mitogenic potency. In accordance with the equivalent in vitro profiles, the toxico-pharmacological properties of...Keywords
This publication has 32 references indexed in Scilit:
- Insulin analogs with improved pharmacokinetic profilesAdvanced Drug Delivery Reviews, 1999
- Intensive blood-glucose control with sulphonylureas or insulin compared with conventional treatment and risk of complications in patients with type 2 diabetes (UKPDS 33)The Lancet, 1998
- Effect of intensive blood-glucose control with metformin on complications in overweight patients with type 2 diabetes (UKPDS 34)The Lancet, 1998
- Interactions of Phenol and m-Cresol in the Insulin Hexamer, and Their Effect on the Association Properties of B28 Pro → Asp Insulin AnaloguesBiochemistry, 1998
- The Effect of Intensive Treatment of Diabetes on the Development and Progression of Long-Term Complications in Insulin-Dependent Diabetes MellitusNew England Journal of Medicine, 1993
- Altering the association properties of insulin by amino acid replacementProtein Engineering, Design and Selection, 1992
- Monomeric Insulins and Their Experimental and Clinical ImplicationsDiabetes Care, 1990
- Monomeric insulins obtained by protein engineering and their medical implicationsNature, 1988
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free systemNature, 1982
- Insulin: The Structure in the Crystal and its Reflection in Chemistry and Biology byAdvances in Protein Chemistry, 1972