Photochromic polypeptides as synthetic models of biological photoreceptors: A spectroscopic study (Articolo in rivista)

Type
Label
  • Photochromic polypeptides as synthetic models of biological photoreceptors: A spectroscopic study (Articolo in rivista) (literal)
Anno
  • 1998-01-01T00:00:00+01:00 (literal)
Alternative label
  • Angelini, N (Angelini, N); Corrias, B (Corrias, B); Fissi, A (Fissi, A); Pieroni, O (Pieroni, O); Lenci, F (Lenci, F) (1998)
    Photochromic polypeptides as synthetic models of biological photoreceptors: A spectroscopic study
    in Biophysical journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Angelini, N (Angelini, N); Corrias, B (Corrias, B); Fissi, A (Fissi, A); Pieroni, O (Pieroni, O); Lenci, F (Lenci, F) (literal)
Pagina inizio
  • 2601 (literal)
Pagina fine
  • 2610 (literal)
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  • 74 (literal)
Rivista
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  • 5 (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • CNR, Ist Biofis, I-56127 Pisa, Italy Univ Sassari, I-07100 Sassari, Italy Univ Pisa, Dept Chem, I-56100 Pisa, Italy (literal)
Titolo
  • Photochromic polypeptides as synthetic models of biological photoreceptors: A spectroscopic study (literal)
Abstract
  • L-Glutamic acid polypeptides containing photochromic nitrospiropyran bound to the side chains at various percentages (\"local\" concentration) have been synthesized and investigated as possible artificial models of biological photoreceptors. Absorption and fluorescence spectroscopy have been utilized to investigate the photophysical and photochemical properties of nitrospiropyrans, both inserted in the polypeptide chain and in solution as \"free\" dye. Conformational variations produced by dark storage and light exposure of the photochromic polypeptides have been studied by means of circular dichroism. Dark-kept \"free\" dyes in hexafluoro-2-propanol solution in the merocyanine form (\"open\" form) give rise to molecular aggregates, which have been characterized as merocyanine dimers. The equilibrium constant between the monomer and the dimer, K, and their molar extinction coefficients, epsilon, at several wavelengths have been determined. Fluorescence measurements on \"free\" and polypeptide-bound nitrospiropyrans suggest that the dimerization process between merocyanines is favored when the photochromic units are inserted in the polypeptide chain and that under these conditions an efficient energy transfer from the monomer (donor) to the dimer (acceptor) occurs. By varying \"local\" as well as total nitrospiropyran concentration, it has been shown that the dimeric species result from intermolecular interactions between photochromic groups inserted in the same polypeptide chain. The alpha-helix --> random coil transition of the polypeptide structure after dark storage has eventually been shown to be the result of the dimerization process and not of the dark isomerization per se from the \"closed\" spiropyran form to the \"open\" merocyanine form of the dye. (literal)
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