Producing wheat gluten gels with tunable mechanical properties via simple sol-gel routes would facilitate their processing into plant protein-rich food products. However, standard gluten is a very elastic mass with a high concentration of proteins in water and is hardly processable except using high shear harsh extrusions. The wheat proteins are responsible for the viscoelastic properties of standard gluten and dough and are among the most complex proteins families, with extremely broad polymorphisms and polydispersities. They are moreover insoluble in water, rendering rational studies difficult. Thanks to a novel protocol for the gluten proteins extraction that we have recently developed, stable ethanolic suspensions of gluten proteins are obtained for a wide range of protein concentrations. In this talk, we will present the viscoelasticity of those suspensions and show that they exhibit a spontaneous and concentration-dependent gelation, which we find to be driven by the slow formation of hydrogen bonds. We successfully rationalize our data using percolation models and relate the viscoelasticity of the gels to their fractal dimension measured by scattering techniques. The novel gluten gels display self-healing properties and their elastic plateaus cover several decades, from 10-2 to 104 Pa. In particular very soft gels as compared to standard hydrated gluten, suitable for processing, can be produced.