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This study is concerned with behaviour of fluid of monoclonal antibodies(mAbs) when trapped in a confinement represented by rigid spherical obstaclesthat attract proteins. The antibody molecule is depicted as an assembly ofseven hard spheres, organized to resemble Y shaped molecule. The antibody hastwo Fab and one Fc domains located in the corners of letter Y. In thiscalculation, only the Fab-Fab and Fab-Fc attractive pair interactions areeffective. The confinement is formed by the randomly distributed hard-spheresfixed in space. The spherical obstacles, besides the size exclusion, alsointeract by the Yukawa attractive interaction with with each bead of theantibody molecule. We applied the combination of the scaled-particle theory,Wertheim's thermodynamic perturbation theory and the Flory-Stockmayer theory tocalculate: (i) the liquid-liquid phase separation, and (ii) the percolationthreshold. All these quantities were calculated as functions of the strength ofthe attraction between the monoclonal antibodies, and monoclonal antibodies andobstacles. The conclusion is that while the hard-sphere obstacles decrease thecritical density as also, the critical temperature of the mAbs fluid, theeffect of the protein-obstacle attraction is more complex. Adding theattraction to obstacle-mAbs interaction first increases the wideness of thetemperature-density envelope. However, with the further increase of theobstacle-mAbs attraction intensity we observe reversal of the effect, thetemperature-density curves become narrower. At some point, depending on theAC=BC interaction, the situation is observed where two different temperatureshave the same fluid density (reentry point ). In all the cases shown here thecritical point decreases below the value for the neat fluid, but the behaviourwith respect to increase of the strength of obstacle-mAbs attraction is notmonotonic.

Behaviour of the model antibody fluid constrained by rigid spherical obstacles. Effects of the obstacle--antibody attraction