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Neural Regulation

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Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

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Published on: January 5, 2016

M14 substitutions in exanatide modulate alpha-synuclein aggregation.

Venkataharsha Panuganti¹, Kanika Manchanda², Prasad V Bharatam^2,3

¹Department of Biotechnology, National Institute of Pharmaceutical Education and Research, S.A.S. Nagar, Punjab, India.

The FEBS Journal

|November 9, 2025

Summary

Exenatide mutants show potential in inhibiting alpha-synuclein aggregation, a key factor in Parkinson's disease (PD). These modified peptides may offer new therapeutic avenues for neurodegenerative disorders by promoting cell survival and autophagy.

Keywords:

Parkinson's disease diabetes mellitus exenatide protein aggregation

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Published on: May 30, 2015

Area of Science:

Neuroscience
Biochemistry
Pharmacology

Background:

Type 2 diabetes (T2DM) and Parkinson's disease (PD) share pathway dysregulation.
Antidiabetic drugs, like exenatide, show neuroprotective effects in PD models.
Exenatide, a GLP1R agonist, crosses the blood-brain barrier and improves PD symptoms in rodents.

Purpose of the Study:

Investigate exenatide's effect on alpha-synuclein aggregation.
Explore how modifications at exenatide's M14 position impact aggregation.
Assess the therapeutic potential of exenatide mutants in PD models.

Main Methods:

Substitution mutations were introduced at the M14 position of exenatide.
In vitro aggregation assays of recombinant human alpha-synuclein were performed.
SH-SY5Y cells were used to study aggregation and cell survival.
Molecular dynamic (MD) simulations and flow cytometry were employed.

Main Results:

Exenatide alone did not affect alpha-synuclein aggregation in vitro.
The M14K exenatide mutant stabilized alpha-synuclein and reduced aggregation.
All exenatide mutants attenuated alpha-synuclein aggregation in SH-SY5Y cells, increasing cell survival.
Peptide treatment induced autophagy, contributing to reduced protein aggregation.

Conclusions:

Exenatide's M14 modifications can influence alpha-synuclein stability and aggregation.
Exenatide and its mutants demonstrate neuroprotective effects in cellular PD models.
Induction of autophagy is a key mechanism for exenatide-mediated reduction of protein aggregation.
Exenatide mutants warrant further investigation as potential alpha-synuclein aggregation inhibitors for PD treatment.