We introduce a new method for the stabilization of colloidal particles via the synthesis and adsorption of unnatural proteins. Biosynthesis of protein-based polymers offers the advantages of preparation of complex sequences through control of the primary sequence, monodisperse polymers, ease of combinatorial search for anchor blocks, environmentally friendly synthesis, use of water as the solvent, and incorporation of a palette of known natural proteins. We have synthesized an unnatural protein with the sequence thioredoxin-Pro(39)Glu(10) for modification of the forces between alumina particles. The polyglutamate sequence, Glu(10), is anionic (pH >3) and is designed to anchor the protein to positively charged solids, e.g. alumina in water (pH <9). The polyproline sequence, Pro(39), is neutral. The thioredoxin is a recombinant form of the natural globular protein with a histidine patch (His-patch-thioredoxin) and is zwitterionic. The combined thioredoxin-Pro(39) sequence is hydrophilic with pI similar to6.3. This block is designed to remain in solution, thereby providing a steric barrier to the approach of two particles in a range of salt and pH conditions. Ellipsometry experiments show that thioredoxin-Pro(39)Glu(10) does adsorb to alumina. Force measurements with the atomic force microscopy (AFM) colloid probe technique show that adsorption of thioredoxin-Pro(39)Glu(10) leads to repulsive forces that decay exponentially with the separation between the surfaces and are independent of salt concentration in the range 0.001-0.1 MKNO3. This demonstrates that the repulsive forces are not electrostatic. We hypothesize that the repulsion is due to confinement and loss of solvent for the adsorbed polymer; the forces are similar to those expected for a polymer brush. Force measurements between thioredoxin-coated alumina surfaces also show a repulsive force, but the force has a decay length that is consistent with electrostatic double-layer forces: the thioredoxin has not neutralized the surface charge of the underlying alumina. Our results point to interesting future experiments where recombinant DNA technology could be used to synthesize fusion proteins containing useful natural proteins and an anchor. This may allow preparation, via single-step aqueous self-assembly, of anchored proteins that maintain their natural structure. Our technique is not limited to homopolymer blocks; more complex primary sequences can be used.