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Soluble Peptide X (also known as soluble Ninjurin-1 or sNinj1) is the soluble, cleaved extracellular domain of Ninjurin-1 (Ninj1), an adhesion molecule originally identified for its role in peripheral nerve regeneration. Ninjurin-1 is cleaved by matrix metalloproteinase-9 (MMP-9) to release sNinj1, which acts as an anti-inflammatory and atheroprotective agent. Soluble Peptide X (sNinj1) and its mimetic peptides (such as ML56 and PN12) function by binding to membrane-bound Ninjurin-1, thereby inhibiting homophilic Ninjurin-1 interactions, suppressing macrophage activation, and reducing monocyte transendothelial migration. In preclinical models, sustained-release formulations of sNinj1 (such as PLGA microspheres/nanoparticles) have demonstrated therapeutic potential in attenuating post-infarction adverse cardiac remodeling and reducing atherosclerosis by suppressing inflammatory cell infiltration and myocardial fibrosis.
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