Oriented Prion Protein Immobilization at Nanostructured Interfaces

Abstract

Even in physiological environment, proteins experience spatial constrains that affect the thermodynamics and kinetics of folding and, as a consequence, their activity. Artificial confinement of proteins can be introduced by patterning proteins on surfaces. Our aim is to provide nanoscaled spots to capture recombinant mouse prion protein residue 89 to 230 recMoPrP(89-230) in an oriented and controlled manner and to study the effect of such confinement on the system activity. We chose Atomic Force Microscopy, one of the foremost tools for imaging, measuring and manipulating matter at the nanoscale, to control molecular density and orientation during spot fabrication, and to detect binding events on the receptors structure by height measurements, without any labeling.