Citation
Volný, Michael; Elam, W. Timothy; Branca, Andrew; Ratner, Buddy D.; & Tureček, František (2005).
Preparative Soft and Reactive Landing of Multiply Charged Protein Ions on a Plasma-Treated Metal Surface.
Anal Chem, 77(15), 4890-4896.
Abstract
Soft landing on a plasma-treated metal surface of multiply protonated protein ions from the gas phase results in a substantial retention of protein function, as demonstrated for trypsin and streptavidin. The majority of trypsin ions soft-landed at hyperthermal kinetic energies are undamaged and retain 72?98% of enzymatic activity after being washed into solution. A small fraction of trypsin ions that were landed at nominal kinetic energies of 130?200 eV remain tethered to the surface and show ?50% enzymatic activity. The streptavidin tetramer is found to dissociate to monomer units upon multiple charging in electrospray. The majority of soft-landed monomers can be washed into solution where they show affinity to biotin. The layer of streptavidin monomer that is immobilized on the surface can be detected if fluorescence-tagged and retains the ability to reversibly bind biotin. A mechanism is proposed to explain nondestructive protein ion discharge on the surface that considers proton migration from the soft-landed cations to the metal oxide layer and metal ion reduction by electron transfer from the bulk metal.
Reference Type
Journal Article
Secondary Title
Anal Chem
Author(s)
Volný, MichaelElam, W. TimothyBranca, AndrewRatner, Buddy D.Tureček, František
Year Published
2005
Date Published
1122854400
Volume Number
77
Issue Number
15
Pages
4890-4896
DOI
10.1021/ac0507136
