High-Affinity Dimeric Inhibitors Designed to Interfere Between Inhibitory Receptors

Dimeric peptides have been developed to interact between gephyrin and inhibitory neurotransmitting receptors.

The brain has Gephyrin, a central scaffolding protein for inhibitory neurotransmitter receptors.

A neurotransmitter receptor is a membrane receptor protein, activated by a neurotransmitter.

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A membrane protein interacts with the phospholipid bilayer that encloses the cell and a membrane receptor protein interacts with a chemical in the cells external environment, which binds to the cell.

Membrane receptor proteins, in neuronal and glial cells, allow cells to communicate with one another through chemical signals.

The development of dimeric peptides inhibits the interaction between gephyrin and these receptors.

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It is a process, which is fundamental to numerous synaptic functions and diseases of the brain.

Receptor-derived minimal gephyrin-binding peptides were identified. It displayed exclusive binding towards native gephyrin from brain lysates.

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A series of dimeric ligands were designed and synthesized, which led to a remarkable 1220-fold enhancement of the gephyrin affinity.

The crystal structures were visualized in X-ray and the simultaneous dimer-to-dimer binding in atomic detail, revealing compound-specific binding modes.

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The molecular basis of the affinity-enhancing effect of multivalent gephyrin inhibitors and novel compounds with therapeutic potential, which will allow further elucidation of the gephyrin–receptor interplay was also defined.

Source-Medindia