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001-es BibID:BIBFORM059572
Első szerző:Bene László (biofizikus)
Cím:Nanoparticle energy transfer on the cell surface / László Bene, Gergely Szentesi, László Mátyus, Rezső Gáspár, Sándor Damjanovich
Dátum:2005
ISSN:0952-3499
Megjegyzések:Membrane topology of receptors plays an important role in shaping transmembrane signalling of cells. Among the methods used for characterizing receptor clusters, fluorescence resonance energy transfer between a donor and acceptor fluorophore plays a unique role based on its capability of detecting molecular level (2-10 nm) proximities of receptors in physiological conditions. Recent development of biotechnology has made possible the usage of colloidal gold particles in a large size range for specific labelling of cells for the purposes of electron microscopy. However, by combining metal and fluorophore labelling of cells, the versatility of metal-fluorophore interactions opens the way for new applications by detecting the presence of the metal particles by the methods of fluorescence spectroscopy. An outstanding feature of the metal nanoparticle-fluorophore interaction is that the metal particle can enhance spontaneous emission of the fluorophore in a distance-dependent fashion, in an interaction range essentially determined by the size of the nanoparticle. In our work enhanced fluorescence of rhodamine and cyanine dyes was observed in the vicinity of immunogold nanoparticles on the surface of JY cells in a flow cytometer. The dyes and the immunogold were targetted to the cell surface receptors MHCI, MHCII, transferrin receptor and CD45 by monoclonal antibodies. The fluorescence enhancement was sensitive to the wavelength of the exciting light, the size and amount of surface bound gold beads, as well as the fluorophore-nanoparticle distance. The intensity of 90 degrees scattering of the incident light beam was enhanced by the immunogold in a concentration and size-dependent fashion. The 90 degrees light scattering varied with the wavelength of the incident light in a manner characteristic to gold nanoparticles of the applied sizes. A reduction in photobleaching time constant of the cyanine dye was observed in the vicinity of gold particles in a digital imaging microscope. Modulations of 90 degrees light scattering intensity and photobleaching time constant indicate the role of the local field in the fluorescence enhancement. A mathematical simulation based on the electrodynamic theory of fluorescence enhancement showed a consistency between the measured enhancement values, the inter-epitope distances and the quantum yields. The feasibility of realizing proximity sensors operating at distance ranges larger than that of the conventional Forster transfer is demonstrated on the surface of living cells
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Antibodies
Antibodies,Monoclonal
Antigens,CD45
B-Lymphocytes
Biophysics
Carbocyanines
Cell Membrane
Cells
Cultured
chemistry
diagnostic use
Dyes
Energy Transfer
Fluorescence
Fluorescent Dyes
Gold
Humans
Hungary
immunology
Light
metabolism
methods
Microscopy
Nanotechnology
Photobleaching
Receptors,Transferrin
Research
Rhodamines
Spectrometry,Fluorescence
Support
Megjelenés:Journal Of Molecular Recognition. - 18 : 3 (2005), p. 236-253. -
További szerzők:Szentesi Gergely (1976-) (kémia-fizika tanár) Mátyus László (1956-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:OTKA-T042618
OTKA
OTKA-TS040773
OTKA
OTKA-T043509
OTKA
OTKA-T043087
OTKA
Internet cím:Szerző által megadott URL
DOI
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2.

001-es BibID:BIBFORM033278
035-os BibID:PMID:8588941 WOS:A1995TF18900001
Első szerző:Vereb György (biofizikus, orvos)
Cím:Plasma-membrane-bound macromolecules are dynamically aggregated to form non-random codistribution patterns of selected functional elements. Do pattern recognition processes govern antigen presentation and intercellular interactions? / György Vereb, László Matyus, László Bene, György Panyi, Zsolt Bacsó, Margit Balázs, János Matkó, János Szöllősi, Rezső Gáspár, Sándor Damjanovich, Robert E. Dale, Carlo Pieri, Marcel Ameloot
Dátum:1995
Megjegyzések:Molecular recognition processes between cell surface elements are discussed with special reference to cell surface pattern formation of membrane-bound integral proteins. The existence, as detected by flow cytometric resonance energy transfer (Appendix), and significance of cell surface patterns involving the interleukin-2 receptor, the T-cell receptor-CD3 system, the intercellular adhesion molecule ICAM-1, and the major histocompatibility complex class I and class II molecules in the plasma membrane of lymphocytes are described. The modulation of antigen presentation by transmembrane potential changes is discussed, and a general role of transmembrane potential changes, and therefore of ion channel activities, adduced as one of the major regulatory mechanisms of cell-cell communication. A general role in the mediation and regulation of intercellular interactions is suggested for cell-surface macromolecular patterns. The dynamic pattern of protein and lipid molecules in the plasma membrane is generated by the genetic code, but has a remarkable flexibility and may be one of the major instruments of accommodation and recognition processes at the cellular level.
Tárgyszavak:Orvostudományok Egészségtudományok idegen nyelvű folyóiratközlemény külföldi lapban
cell surface
molecular pattern
energy transfer
fluorescence
flow cytometry
transmembrane potential
MHC
antigen presentation
intercellular communication
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Molecular Recognition. - 8 : 4 (1995), p. 237-246. -
További szerzők:Mátyus László (1956-) (biofizikus) Bene László (1963-) (biofizikus) Panyi György (1966-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Dale, Robert E. Pieri, Carlo Ameloot, Marcel
Internet cím:DOI
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