VnP-16, a synthetic peptide fragment mirroring amino acids 270-281 of vitronectin (a multifunctional glycoprotein involved in cell attachment, migration, and spreading), promotes attachment and spreading of isolated human osteogenic cells. This effect is reversible with β1 integrin siRNA knockdown when VnP-16 is applied at 9.1 µg/cm2 on cell plates. The compound enhances osteogenesis in human skin-derived mesenchymal precursors and MC3T3-E1 mouse calvarial osteoblast precursors. Furthermore, in vivo studies show VnP-16 mitigates IL-1α-induced bone loss, reduces calvarial osteoclast numbers in mice, increases bone mineral density, and lessens trabecular bone loss in a mouse model of ovariectomy-induced bone loss.

Vasonatrin peptide (VNP) is a chimera of atrial natriuretic peptide (ANP) and C-type natriuretic peptide (CNP) with potent venodilating and natriuretic activity.

Vasonatrin Peptide (VNP) TFA, a chimeric compound derived from atrial natriuretic peptide (ANP) and C-type natriuretic peptide (CNP), exhibits venodilating properties reminiscent of CNP, natriuretic effects akin to ANP, as well as unique arterial vasodilating capabilities not characteristic of either parent peptide. Additionally, VNP TFA confers cardioprotection in diabetic ischemia-reperfusion injury by attenuating endoplasmic reticulum (ER) stress through the cGMP-PKG signaling cascade [1] [2] [3].

VnP-16 enhances bone formation by stimulating the differentiation and activity of osteoblasts via direct β1 integrin engagement, which subsequently activates FAK [1].