This work compares the spreading and relaxation rates of albumin and fibrinogen, inferred from single-component and competitive adsorption kinetic experiments, on model. surfaces of varying hydrophobicity. Kinetics from the single-component studies revealed a constant spreading rate, where the adsorbed protein footprint grew linearly in time for at least 15 min. This spreading rate increased with substrate hydrophobicity (ranging from 0.02 to 0.16 nm(2)/molecule/s for albumin and from 0.04 to 0.26 nm(2)/molecule/s for fibrinogen), resulting in a larger extent of footprint growth and a lower ultimate coverage on hydrophobic surfaces when compared with hydrophilic surfaces at the same adsorption conditions. Competitive adsorption studies were in qualitative agreement with the single-component experiments but were able to probe longer spreading time scales. Although spreading appeared to occur initially at a constant rate in the competitive experiments, after 2 h the spreading rate had slowed dramatically and the spreading process had begun to level off.