Abstract
Although interaction of human insulin with its receptor is studied to considerable extent such studies are currently lacking with recombinant insulin in-spite of its rampant clinical use. It is known that at molecular level the interaction of recombinant insulin with insulin receptor is similar to human insulin but not exactly same. With the increasing incidence of diabetes throughout the globe use of recombinant insulin is also increasing at a considerable rate. Therefore it is need of the hour to explore the recombinant insulin- insulin receptor interaction by all possible means. In this paper we have studied insulin receptor binding of lispro and glargine; the two commonly used recombinant insulins using tools of computational biology. We have observed that the binding pattern of insulin receptor (L1-CR-L2 ectodomain) with lispro and glargine is different when compared with human insulin. Analyzing the ligand receptor interactions we have hypothesized that the tail region of insulin beyond B26 is a critical regulator of insulin insulin receptor interactions detail of which cannot be understandable from docking studies due to lack of consideration of the flexibility of the tail region while docking studies. We have recommended experimental validation of our study. However, our docking procedure may also be explored for preliminary screening of novel anti-diabetic peptide.
Highlights
Interaction of human insulin with its receptor is studied to considerable extent such studies are currently lacking with recombinant insulin in-spite of its rampant clinical use
In-vitro studies have confirmed that L1-CR-L2 ectodomain of insulin receptor binds with insulin with considerable affinity [9] without participation of alpha CT region of insulin receptor which may be required for insulin binding to IR in-vivo [10]
There is evidence that receptor binding affinity of lispro and glargine is less than normal human insulin [6]
Summary
Interaction of human insulin with its receptor is studied to considerable extent such studies are currently lacking with recombinant insulin in-spite of its rampant clinical use. Taking into consideration therapeutic efficacy of insulin lispro and insulin glargine are many limitations of such understanding theoretical modeling considered to be proved and they are in regular clinical use but studies have been published to develop a model of such biological functions are not exactly identical to human insulin interactions [3]. Such studies are critical taking into when mutagenicity or receptor binding affinity of consideration the wide spread emergence of diabetes mellitus the above molecules are concerned [6]. In this work we are reporting insulin receptor (L1-CR-L2 ectodomain), insulin lispro and insulin glargine interactions in comparison with human insulin using tools of computational biology
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