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

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

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  • 1School of Pharmaceutical Sciences, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu 214122, PR China.
  • 2School of Pharmaceutical Sciences, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu 214122, PR China; Institute of Health Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences and Shanghai Jiao-Tong University School of Medicine, 320 Yue-Yang Road, Shanghai 200031, PR China. Electronic address:


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.

Copyright © 2014 Elsevier Inc. All rights reserved.


Binding affinity; Molecular dynamics; Natriuretic peptide; Natriuretic peptide receptor; Vasonatrin peptide

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