FFC#4/2014

The molecular structure and the folding of the whole Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): correctors sites

AREA 1 Therapies to correct the underlying defect

FFC#4/2014

The molecular structure and the folding of the whole Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): correctors sites
€ 0 still needed
0%
€ 45.000 goal

pRINCIPAL INVESTIGATOR

Oscar Moran (Istituto di Biofisica, Consiglio Nazionale delle Ricerche – CNR, Genova)

Researchers

5

Category

AREA 1 Therapies to correct the underlying defect

Duration

2 years

Goal

€ 45.000

Funds raised

€ 45.000

Objectives

Proteins’ function strictly depends on their three-dimensional conformation. Therefore, details in the structure of CFTR, responsible for Cystic Fibrosis, may be important knowledge to the understanding of its function. This project aims to study the molecular structure of CFTR using small-angle X-ray scattering. With this technique, which does not require any particular treatment of the sample, it is possible to obtain detailed information on the molecular structure of proteins under conditions similar to physiological ones. The structures of the normal CFTR and CFTR carrying the F508del mutation were compared and how correctors modified the molecular conformation of the mutant was deeply investigated. These informations may help to develop new correctors designed in a more rationale way.

WHO ADOPTED THE PROJECT

Delegazione FFC di Bologna

€ 45.000

Delegazione FFC di Imola e Romagna

€ 30.000

Gli Amici per la Ricerca di Bassano 2014

€ 25.000

OTHER PROJECTS

Discover the other projects

GMRF#1/2026

Exploring the role of PKD1 in promoting CFTR stability and function at the cell surface

FFC#1/2026

Mapping proteins regulating CFTR mRNA stability to identify new therapeutic targets for nonsense mutations

FFC#2/2026

Evaluating the potential of phosphodiesterase inhibitors to enhance the efficacy of CFTR modulators and support personalized therapeutic approaches