Computer‐assisted engineering of hyperstable fibroblast growth factor 2
Citations Over TimeTop 11% of 2017 papers
Abstract
Fibroblast growth factors (FGFs) serve numerous regulatory functions in complex organisms, and their corresponding therapeutic potential is of growing interest to academics and industrial researchers alike. However, applications of these proteins are limited due to their low stability. Here we tackle this problem using a generalizable computer-assisted protein engineering strategy to create a unique modified FGF2 with nine mutations displaying unprecedented stability and uncompromised biological function. The data from the characterization of stabilized FGF2 showed a remarkable prediction potential of in silico methods and provided insight into the unfolding mechanism of the protein. The molecule holds a considerable promise for stem cell research and medical or pharmaceutical applications.
Related Papers
- → Control of Fibroblast Growth Factor (FGF) 7- and FGF1-induced Mitogenesis and Downstream Signaling by Distinct Heparin Octasaccharide Motifs(2006)38 cited
- → The Heterohexameric Complex Structure, a Component in the Non-classical Pathway for Fibroblast Growth Factor 1 (FGF1) Secretion(2010)29 cited
- → Structure of rat acidic fibroblast growth factor at 1.4 Å resolution(2007)2 cited
- → Molecular Level Interaction of the Human Acidic Fibroblast Growth Factor with the Antiangiogenic Agent, Inositol Hexaphosphate,(2010)5 cited
- → A molecular dynamics study of the FGF1/FGF2 heterodimer in human fibroblasts(2023)1 cited