Quantitative analysis of protein adsorption via atomic force microscopy and surface plasmon resonance.
Surface properties have a significant influence on the performance of biomedical devices. The influence of surface chemistry on the amount and distribution of adsorbed proteins has been evaluated by a combination of atomic force microscopy (AFM) and surface plasmon resonance (SPR). Adsorption of albumin, fibrinogen, and fibronectin was analyzed under static and dynamic conditions, employing self-assembled monolayers (SAMs) as model surfaces. AFM was performed in tapping mode with antibody-modified tips. Phase-contrast images showed protein distribution on SAMs and phase-shift entity provided information on protein conformation. SPR analysis revealed substrate-specific dynamics in each system investigated. When multi-protein solutions and diluted human plasma interacted with SAMs, SPR data suggested that surface chemistry governs the equilibrium composition of the protein layer.
Servoli
Eva
E
Department of Materials Engineering and INSTM Research Unit, University of Trento, Trento, Italy. servolie@ing.unitn.it
Maniglio
Devid
D
Aguilar
Maria Rosa
MR
Motta
Antonella
A
San Roman
Julio
J
Belfiore
Laurence A
LA
Migliaresi
Claudio
C
D000327:Adsorption; D018625:Microscopy, Atomic Force / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D020349:Surface Plasmon Resonance / Q000379:methods*
D011506:Proteins