bOptimizing atomic force microscopy for characterization of diamond-protein interfaces
Status PubMed-not-MEDLINE Language English Country United States Media electronic
Document type Journal Article
PubMed
21711846
PubMed Central
PMC3211425
DOI
10.1186/1556-276x-6-337
PII: 1556-276X-6-337
Knihovny.cz E-resources
- Publication type
- Journal Article MeSH
Atomic force microscopy (AFM) in contact mode and tapping mode is employed for high resolution studies of soft organic molecules (fetal bovine serum proteins) on hard inorganic diamond substrates in solution and air. Various effects in morphology and phase measurements related to the cantilever spring constant, amplitude of tip oscillations, surface approach, tip shape and condition are demonstrated and discussed based on the proposed schematic models. We show that both diamond and proteins can be mechanically modified by Si AFM cantilever. We propose how to choose suitable cantilever type, optimize scanning parameters, recognize and minimize various artifacts, and obtain reliable AFM data both in solution and in air to reveal microscopic characteristics of protein-diamond interfaces. We also suggest that monocrystalline diamond is well defined substrate that can be applicable for fundamental studies of molecules on surfaces in general.
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