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Targeting different binding sites in the CFTR structures allows to synergistically potentiate channel activity.

Abstract：

:Recent evidence shows that combination of correctors and potentiators, such as the drug ivacaftor (VX-770), can significantly restore the functional expression of mutated Cystic Fibrosis Transmembrane conductance Regulator (CFTR), an anion channel which is mutated in cystic fibrosis (CF). The success of these combinatorial therapies highlights the necessity of identifying a broad panel of specific binding mode modulators, occupying several distinct binding sites at structural level. Here, we identified two small molecules, SBC040 and SBC219, which are two efficient cAMP-independent potentiators, acting at low concentration of forskolin with EC50 close to 1 μM and in a synergic way with the drug VX-770 on several CFTR mutants of classes II and III. Molecular dynamics simulations suggested potential SBC binding sites at the vicinity of ATP-binding sites, distinct from those currently proposed for VX-770, outlining SBC molecules as members of a new family of potentiators.

journal_name

Eur J Med Chem

journal_title

European journal of medicinal chemistry

authors

Froux L,Elbahnsi A,Boucherle B,Billet A,Baatallah N,Hoffmann B,Alliot J,Zelli R,Zeinyeh W,Haudecoeur R,Chevalier B,Fortuné A,Mirval S,Simard C,Lehn P,Mornon JP,Hinzpeter A,Becq F,Callebaut I,Décout JL

doi

10.1016/j.ejmech.2020.112116

subject

Has Abstract

pub_date

2020-03-15 00:00:00

pages

112116

eissn

0223-5234

issn

1768-3254

pii

S0223-5234(20)30083-0

journal_volume

190

pub_type

杂志文章

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