Thermal Transitions of Fibrillar Collagen Unveiled by Second-Harmonic Generation Microscopy of Corneal Stroma (Articolo in rivista)

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  • Thermal Transitions of Fibrillar Collagen Unveiled by Second-Harmonic Generation Microscopy of Corneal Stroma (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bpj.2012.07.055 (literal)
Alternative label
  • Matteini Paolo [ 1 ] ; Cicchi Riccardo [ 2,3 ] ; Ratto Fulvio [ 1 ] ; Kapsokalyvas Dimitrios [ 3 ] ; Rossi Francesca [ 1 ] ; de Angelis Marella [ 1 ] ; Pavone Francesco S. [ 3 ] ; Pini Roberto [ 1 ] (2012)
    Thermal Transitions of Fibrillar Collagen Unveiled by Second-Harmonic Generation Microscopy of Corneal Stroma
    in Biophysical journal (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Matteini Paolo [ 1 ] ; Cicchi Riccardo [ 2,3 ] ; Ratto Fulvio [ 1 ] ; Kapsokalyvas Dimitrios [ 3 ] ; Rossi Francesca [ 1 ] ; de Angelis Marella [ 1 ] ; Pavone Francesco S. [ 3 ] ; Pini Roberto [ 1 ] (literal)
Pagina inizio
  • 1179 (literal)
Pagina fine
  • 1187 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 103 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 6 (literal)
Note
  • PubMe (literal)
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
  • Google Scholar (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • [ 1 ] CNR, Inst Appl Phys Nello Carrara, Sesto Fiorentino, Italy [ 2 ] CNR, Natl Inst Opt, Florence, Italy [ 3 ] European Lab Nonlinear Spect, LENS, Sesto Fiorentino, Italy (literal)
Titolo
  • Thermal Transitions of Fibrillar Collagen Unveiled by Second-Harmonic Generation Microscopy of Corneal Stroma (literal)
Abstract
  • The thermal transitions of fibrillar collagen are investigated with second-harmonic generation polarization anisotropy microscopy. Second-harmonic generation images and polarization anisotropy profiles of corneal stroma heated in the 35-80°C range are analyzed by means of a theoretical model that is suitable to probe principal intramolecular and interfibrillar parameters of immediate physiological interest. Our results depict the tissue modification with temperature as the interplay of three destructuration stages at different hierarchical levels of collagen assembly including its tertiary structure and interfibrillar alignment, thus supporting and extending previous findings. This method holds the promise of a quantitative inspection of fundamental biophysical and biochemical processes and may find future applications in real-time and postsurgical functional imaging of collagen-rich tissues subjected to thermal treatments. (literal)
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