Fig. 2: LCDV1-VILP as a single chain peptide is more potent to bind on IGF1R and on IR.
From: Interaction of a viral insulin-like peptide with the IGF-1 receptor produces a natural antagonist
Competition binding assays on human IGF1R (a) and human IR (b) ectodomains. Data are expressed as the mean ± SEM, normalized to the baseline and expressed as % of the maximal binding of 125I-IGF-1 (a) and 125I-Insulin (b) incubated alone (n = 3 (IGF1R) and 4 (IR) independent wells). Western blot detection of IGF1R, IR, AKT, IRS1, ERK1, and ERK2 phosphorylation in lysates of murine preadipocytes overexpressing the human IGF1R (c) or the human IR (d). Quantitative analysis of phosphorylated IGF1R, IR and AKT. Data, expressed as mean ± SEM (n = 3 independent experiments), were normalized by phosphorylation intensity induced by 10 nM of IGF-1 (e) or insulin (f).
