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@ARTICLE{Polovinkin:185982,
      author       = {Polovinkin, V. and Balandin, T. and Volkov, O. and Round,
                      E. and Borshchevskiy, V. and Utrobin, P. and von Stetten, D.
                      and Royant, A. and Willbold, D. and Arzumanyan, G. and
                      Chupin, V. and Popot, J-L and Gordeliy, V.},
      title        = {{N}anoparticle surface-enhanced {R}aman scattering of
                      bacteriorhodopsin stabilized by amphipol {A}8-35},
      journal      = {The journal of membrane biology},
      volume       = {247},
      number       = {9-10},
      issn         = {1432-1424},
      address      = {New York, NY},
      publisher    = {Springer},
      reportid     = {FZJ-2015-00091},
      pages        = {971 - 980},
      year         = {2014},
      abstract     = {Surface-enhanced Raman spectroscopy (SERS) has developed
                      dramatically since its discovery in the 1970s, because of
                      its power as an analytical tool for selective sensing of
                      molecules adsorbed onto noble metal nanoparticles (NPs) and
                      nanostructures, including at the single-molecule (SM) level.
                      Despite the high importance of membrane proteins (MPs), SERS
                      application to MPs has not really been studied, due to the
                      great handling difficulties resulting from the amphiphilic
                      nature of MPs. The ability of amphipols (APols) to trap MPs
                      and keep them soluble, stable, and functional opens up onto
                      highly interesting applications for SERS studies, possibly
                      at the SM level. This seems to be feasible since single
                      APol-trapped MPs can fit into gaps between noble metal NPs,
                      or in other gap-containing SERS substrates, whereby the
                      enhancement of Raman scattering signal may be sufficient for
                      SM sensitivity. The goal of the present study is to give a
                      proof of concept of SERS with APol-stabilized MPs, using
                      bacteriorhodopsin (BR) as a model. BR trapped by APol A8-35
                      remains functional even after partial drying at a low
                      humidity. A dried mixture of silver Lee-Meisel colloid NPs
                      and BR/A8-35 complexes give rise to SERS with an average
                      enhancement factor in excess of 10(2). SERS spectra resemble
                      non-SERS spectra of a dried sample of BR/APol complexes.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25192978},
      UT           = {WOS:000343835500017},
      doi          = {10.1007/s00232-014-9701-9},
      url          = {https://juser.fz-juelich.de/record/185982},
}