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The proteolytic fragment acidic serine- and aspartate-rich motif is highly conserved in the SIBLING family proteins, including osteopontin and matrix extracellular phosphoglycoprotein (MEPE). Of these, the (MEPE) derived phosphorylated ASARM peptide (ASARM) may act as an endogenous anti-mineralization factor. Since ASARM contains unstable amino acid sequences and PHEX cleavage sites, it may exert hypomineralization effects temporally and locally. Therefore, we synthesized and characterized several various ASARM peptide derivatives using in vitro and in vivo systems. The results indicated that ASARM inhibited the formation of calciprotein particles (CPP) involved in an inverse correlation between vascular calcification and bone formation. Besides decreasing vascular calcification in mouse vascular aortic smooth muscle (MOVAS) cells, ASARM-Y inhibited vascular calcification in (Enpp1) (ectonucleotide pyrophosphatase) mutant mice fed a high phosphate diet, a model of generalized artificial calcification of infancy.