Anastellin

Anastellin is a recombinant peptide fragment derived from the C-terminal portion of the first type III repeat of fibronectin (FnIII1) [Morla et al., 1994]. It is characterized by its unique ability to bind to soluble fibronectin and catalyze its conversion into an insoluble, fibrillar form known as superfibronectin, which possesses enhanced cell-adhesive properties [Ambesi et al., 2005]. This induction of superfibronectin effectively alters the extracellular matrix environment, leading to the inhibition of endothelial cell proliferation, migration, and tube formation [Yi and Ruoslahti, 2001]. Consequently, anastellin has been extensively studied in preclinical oncology models for its potent anti-angiogenic and anti-metastatic effects, showing significant suppression of tumor growth [Pasqualini et al., 1996]. Although it is not a traditional receptor or enzyme, it acts as a biological modulator of the extracellular matrix and is considered a promising candidate for peptide-based cancer therapies [Briet et al., 2008].

Other names

FnIII1cFibronectin fragment FnIII1cSuperfibronectin inducer

Anastellin binds to the first type III repeat of fibronectin, inducing a conformational change that leads to the formation of an insoluble, fibrillar matrix known as superfibronectin, which subsequently inhibits endothelial cell proliferation and migration [Morla et al., 1994; Yi and Ruoslahti, 2001].