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ID: ALA4364262

Journal: J Med Chem

Title: PeIA-5466: A Novel Peptide Antagonist Containing Non-natural Amino Acids That Selectively Targets α3β2 Nicotinic Acetylcholine Receptors.

Authors: Hone AJ, Fisher F, Christensen S, Gajewiak J, Larkin D, Whiteaker P, McIntosh JM.

Abstract: Pharmacologically distinguishing α3β2 nicotinic acetylcholine receptors (nAChRs) from closely related subtypes, particularly α6β2, has been challenging due to the lack of subtype-selective ligands. We created analogs of α-conotoxin (α-Ctx) PeIA to identify ligand-receptor interactions that could be exploited to selectively increase potency and selectivity for α3β2 nAChRs. A series of PeIA analogs were synthesized by replacing amino acid residues in the second disulfide loop with standard or nonstandard residues and assessing their activity on α3β2 and α6/α3β2β3 nAChRs heterologously expressed in Xenopus laevis oocytes. Asparagine11 was found to occupy a pivotal position, and when replaced with negatively charged amino acids, selectivity for α3β2 over α6/α3β2β3 nAChRs was substantially increased. Second generation peptides were then designed to further improve both potency and selectivity. One peptide, PeIA-5466, was ∼300-fold more potent on α3β2 than α6/α3β2β3 and is the most α3β2-selective antagonist heretofore reported.

CiteXplore: 31194549

DOI: 10.1021/acs.jmedchem.9b00566