Neutron re?ectivity is a powerful technique for probing adsorbed layers at interfaces. It has been used to investigate proteins adsorbed onto a hydrophilic silica surface. A comparison was made between the protonated and deuterated forms of HSA & MBP. Results show the deuterated proteins to have a higher a?nity for the surface with adsorption occurring in a 3:1 ratio when from a 1:1 mixture. Likewise, d-MBP displaces h-MBP more readily than vice versa in an active exchange process. When investigating binary mixtures lysozyme (LYS) dominates when adsorbed from a mixture with h-HSA but from a d-HSA & LYS mix both proteins were adsorbed. The marked di?erence between the adsorption of perdeuterated and protonated proteins provides a good case study for testing the neutron re?ectivity technique when investigating mixed protein systems. It shows the impact of deuteration on the physicochemical characteristics of the proteins and on the adsorption.

Adsorption of perdeuterated and protonated proteins at the solid/liquid interface: A neutron reflectivity study

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.