Vasonatrin peptide stimulates both of the natriuretic peptide receptors, NPRA and NPRB

Biochem Biophys Res Commun. 2014 Apr 18;446(4):1276-80. doi: 10.1016/j.bbrc.2014.03.110. Epub 2014 Mar 31.

Abstract

Vasonatrin peptide (VNP) is an active cardiovascular factor and a novel synthetic natriuretic peptide with unknown natriuretic peptide receptor (NPR) binding properties. We set out to design binding models of NPRA/VNP and NPRB/VNP, and then assessed their recognition and binding affinities using molecular dynamics. Molecular dynamics analysis indicated decreases in the values of Van der Waals, electrostatic energy and potential energy of NPRB/VNP compared to NPRA/VNP. There was a 25% increase in H-bond formation between VNP and NPRB. The cGMP stimulated by VNP in NPRB-transfected HEK-293 cells was 11-fold higher than that of NPRA. We therefore demonstrated that VNP binds with both NPRA and NPRB, but with a preference for NPRB.

Keywords: Binding affinity; Molecular dynamics; Natriuretic peptide; Natriuretic peptide receptor; Vasonatrin peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Atrial Natriuretic Factor / chemistry
  • Atrial Natriuretic Factor / metabolism*
  • Binding Sites
  • HEK293 Cells
  • Humans
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Receptors, Atrial Natriuretic Factor / chemistry
  • Receptors, Atrial Natriuretic Factor / metabolism*

Substances

  • ventricular natriuretic peptide, eel
  • Atrial Natriuretic Factor
  • Receptors, Atrial Natriuretic Factor
  • atrial natriuretic factor receptor A
  • atrial natriuretic factor receptor B