Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Delving Deep into the Structural Aspects of the BPro28-BLys29 Exchange in Insulin Lispro: A Structural Biophysical Lesson

Wei Li * ORCID logo
Version 1 : Received: 22 July 2020 / Approved: 23 July 2020 / Online: 23 July 2020 (11:45:01 CEST)

How to cite: Li, W. Delving Deep into the Structural Aspects of the BPro28-BLys29 Exchange in Insulin Lispro: A Structural Biophysical Lesson. Preprints 2020, 2020070552 (doi: 10.20944/preprints202007.0552.v1). Li, W. Delving Deep into the Structural Aspects of the BPro28-BLys29 Exchange in Insulin Lispro: A Structural Biophysical Lesson. Preprints 2020, 2020070552 (doi: 10.20944/preprints202007.0552.v1).

Abstract

Insulin lispro was the first fast acting insulin analogue to obtain regulatory approval for therapeutic use. This article puts forward a novel biophysical mechanism where the net impact of the simple B28Pro-B29Lys exchange from regular insulin to insulin lispro is the establishment of a novel set of interfacial electrostatic interactions between Lys28 of insulin lispro and Asp12 of insulin receptor (IR). In addition, a set of structural analysis was presented in this article to further strengthen the binding of insulin lispro to IR, where two polar amino acid residues (Gln51 and Asn74 of insulin lispro) were put forward as two potential targets for site-directed mutagenesis of insulin lispro at its binding interface with IR.

Subject Areas

Insulin lispro; BPro28-BLys29 Exchange; Interfacial biophysics; Structural analysis;

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our diversity statement.

Leave a public comment
Send a private comment to the author(s)
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.