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Enzyme-Linked ImmunoSorbent Assays (ELISA) are a range of widely usedanalytical methods whose implementation requires to build antibodies (IgG) thinfilms onto surfaces predominantly made of polystyrene. The high hydrophobicityof polystyrene ensures a spontaneous and strong adhesion of proteins allowingto easily build IgG monolayers. Since the ELISA improvements definitely lie inthe comprehension of physico-chemical mechanisms on which IgG immobilization onhydrophobic surfaces are relied, this work develops a theorization essay(thermodynamics of the so-called hydrophobic effect and of thin films building)emphasized by numerical modelling (random sequential additions model, i.e. RSA)and experimental estimations by atomic force microscopy (AFM) and ELISA.Keeping in mind the hydrophobic effect, thermodynamics (of irreversibleprocesses) allows to explain why IgG adhesion on polystyrene occurs whereasnumerical modelling approaches show a way of surface saturation leading topromote IgG orientations expected for ELISA. Finally, an improvement of RSA ina RSA+R model taking into account orientational and/or structural changesthroughout relaxation phenomena shows an obvious relationship betweendeposition conditions and obtained monolayer structure. Such theoreticalresults seem to be strongly correlated with experimental facts, i.e. AFM andELISA.

IgG Adhesion on Hydrophobic Surfaces: Theory, Modelling, and Application to ELISA