title: Quantitative analysis of protein adsorption via atomic force microscopy and surface plasmon resonance.
abstract: 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.
authors.affiliation: Department of Materials Engineering and INSTM Research Unit, University of Trento, Trento, Italy. servolie@ing.unitn.it
authors.forename: Eva
authors.initials: E
authors.lastname: Servoli
authors.forename: Devid
authors.initials: D
authors.lastname: Maniglio
authors.forename: Maria Rosa
authors.initials: MR
authors.lastname: Aguilar
authors.forename: Antonella
authors.initials: A
authors.lastname: Motta
authors.forename: Julio
authors.initials: J
authors.lastname: San Roman
authors.forename: Laurence A
authors.initials: LA
authors.lastname: Belfiore
authors.forename: Claudio
authors.initials: C
authors.lastname: Migliaresi
mesh_terms: D000327:Adsorption; D018625:Microscopy, Atomic Force / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D020349:Surface Plasmon Resonance / Q000379:methods*
chemical_list: D011506:Proteins