Design of a Proteolytically Stable Sodium-Calcium Exchanger 1 Activator Peptide for In Vivo Studies.

ABSTRACT: The cardiac sodium-calcium exchanger (NCX1) is important for normal Na⁺- and Ca²⁺-homeostasis and cardiomyocyte relaxation and contraction. It has been suggested that NCX1 activity is reduced by phosphorylated phospholemman (pSer68-PLM); however its direct interaction with PLM is debated. Disruption of the potentially inhibitory pSer68-PLM-NCX1 interaction might be a therapeutic strategy to increase NCX1 activity in cardiac disease. In the present study, we aimed to analyze the binding affinities and kinetics of the PLM-NCX1 and pSer68-PLM-NCX1 interactions by surface plasmon resonance (SPR) and to develop a proteolytically stable NCX1 activator peptide for future in vivo studies. The cytoplasmic parts of PLM (PLM_cyt) and pSer68-PLM (pSer68-PLM_c

SUBMITTER: Wanichawan P 

PROVIDER: S-EPMC8215385 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature