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A_2A Receptor Homodimer-Disrupting Sequence Efficiently Delivered by a Protease-Resistant, Cyclic CPP Vector.

Maria Gallo¹, Gemma Navarro^2,3, Rafael Franco^4,5

¹Department of Experimental and Health Sciences, Pompeu Fabra University, 08003 Barcelona, Spain. maria.gallo@upf.edu.

International Journal of Molecular Sciences

|October 9, 2019

Summary

A novel cyclic peptide effectively disrupts G-protein-coupled receptor (GPCR) oligomerization by targeting transmembrane sequences. This cyclic peptide shows enhanced stability and efficacy compared to its linear form.

Keywords:

GPCR GPCR function adenosine receptors disrupting peptides homodimerization trypsin

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Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

G-protein-coupled receptors (GPCRs) form dimers/oligomers, but their functional significance remains unclear.
Investigating GPCR oligomerization requires methods to disrupt these interactions and assess functional consequences.

Purpose of the Study:

To develop and evaluate a novel cyclic peptide for disrupting GPCR oligomerization.
To compare the efficacy and stability of a cyclic peptide vector against its linear analogue.

Main Methods:

Design and synthesis of a cyclic, Tat-like peptide vector.
Fusion of the cyclic peptide vector to transmembrane domains involved in GPCR oligomerization.
Assessment of peptide efficacy in disrupting receptor oligomerization and functionality.
Evaluation of proteolytic stability using trypsin digestion.

Main Results:

The cyclic Tat-like peptide demonstrated improved efficacy in targeting interreceptor sequences within the transmembrane space compared to linear analogues.
A cyclic Tat-like vector fused to a non-oligomerization-involved transmembrane region was ineffective, confirming target specificity.
The cyclic peptide exhibited enhanced stability against trypsin digestion, indicating increased proteolytic resistance.

Conclusions:

Cyclic peptide design can enhance the targeting and stability of disruptor peptides for GPCRs.
This cyclic peptide represents a promising tool for studying GPCR oligomerization and function.