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Developing a novel exenatide-based incretin mimic (αB-Ex): Expression, purification and structural-functional

Mohammad Mehdi Ghanbarnezhad¹, Mohammad Bagher Shahsavani¹, Pramod S Mali²

¹Protein Chemistry Laboratory (PCL), Department of Biology, College of Sciences, Shiraz University, Shiraz, Iran.

Biochimica Et Biophysica Acta. General Subjects

|April 13, 2022

Summary

Researchers developed a novel hybrid protein, αB-Ex, by combining an exenatide analogue with human αB-crystallin. This new incretin mimic effectively reduces blood sugar and enhances insulin secretion, showing promise for type 2 diabetes mellitus treatment.

Keywords:

Exenatide analogue Incretin activity Mass spectroscopy Secondary structure Type 2 diabetes mellitus (T2DM)αB-Ex hybrid protein

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Area of Science:

Biochemistry and Molecular Biology
Pharmacology and Drug Discovery
Endocrinology and Metabolism

Background:

Glucagon-like peptide-1 (GLP-1) receptor agonists, such as exenatide, are established treatments for type 2 diabetes mellitus (T2DM) and obesity.
There is an ongoing need for novel incretin mimics with improved pharmacokinetic profiles and therapeutic efficacy.
Hybrid protein strategies offer a platform for developing new therapeutic agents with enhanced properties.

Purpose of the Study:

To engineer and characterize a novel hybrid protein (αB-Ex) by conjugating an exenatide analogue to human αB-crystallin.
To evaluate the biological activity of the exenatide analogue and the αB-Ex hybrid protein in vitro and in vivo.
To assess the potential of αB-Ex as a therapeutic candidate for T2DM management.

Main Methods:

Construction and bacterial expression of a fusion protein comprising an exenatide analogue and human αB-crystallin (αB-Ex).
Purification of the exenatide analogue from the hybrid protein using gel filtration chromatography.
Characterization using HPLC, ESI-MS, MALDI-TOF, DLS, and NMR; assessment of blood glucose-lowering and insulin-secreting effects in mice.

Main Results:

High purity (>97%) and accurate molecular mass were confirmed for the exenatide analogue and the αB-Ex hybrid protein.
Spectroscopic analyses indicated distinct secondary structures (α-helix for analogue, β-sheet for αB-Ex), with αB-Ex forming large oligomers.
Both the exenatide analogue and αB-Ex demonstrated significant blood glucose reduction and insulin secretion induction in healthy and diabetic mice.

Conclusions:

The study successfully developed and characterized a novel αB-Ex hybrid protein, a potential long-acting incretin mimic.
αB-Ex exhibits potent glucose-lowering and insulin-stimulating activities, comparable to the exenatide analogue.
The αB-Ex hybrid protein represents a promising drug candidate for the treatment of type 2 diabetes mellitus.