We have used solid-phase peptide synthesis to graft a peptide monolayer from a solid in order to modify the interfacial properties. We grafted a 15-residue peptide, EKEKEKEKEKEKEGG, containing a zwitterionic sequence of alternating lysine and glutamic acid residues from the surface of an aminosilanized silicon wafer by placing the silicon wafer within a commercial microwave peptide synthesizer. Such synthesizers are routinely used to make peptides on porous beads, but the peptides are subsequently cleaved and used independently of the solid support; our aim is to utilize the covalently bound peptide to control the surface properties without the need for cleavage and reattachment. We confirmed the presence of this peptide layer on the surface by X-ray photoelectron spectroscopy and ellipsometry. Atomic force microscopy was then used to study the forces between the peptide-modified surface and a borosilicate glass sphere as a function of the solution pH. The adsorbed peptide makes the silicon wafer pH responsive: at high pH the glass particle is repelled from the wafer, and at low pH it is attracted. Previous studies with synthetic polymers have shown that the "grafting from" method allows a much higher film density than "grafting to". We propose that the application of grafting from strategies to peptide layers may offer three additional benefits: (1) the film density can be controlled independently of the primary sequence of the peptide, (2) the sequence constraints for spontaneous adsorption are removed, and (3) the procedure is fast and efficient, which may lead to lower costs and the ability for high-throughput surface biofunctionalization. Moreover, peptide layers offer increased sequence diversity, control, and functionality compared to conventional polymer brushes.