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UV–Visible absorption spectra of conjugated dienes arise from the lowest energy π → π* transitions. The light-absorbing part of the molecule is called the chromophore, and the substituents directly attached to the chromophore are called auxochromes. A strong correlation exists between the absorption maxima, λmax, and the structure of a conjugated π system. The Woodward–Fieser rules predict the value of λmax for a given...
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Biliverdin's Propionic Chains Influence Oligomerization in Sandercyanin.

Eleftherios Mainas1, Gregory M Curtin1, Shaena D Riddles1

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Sandercyanin, a fluorescent protein, can be improved for bioimaging. Its biliverdin chromophore

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Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Sandercyanin is a tetrameric biliprotein with a non-covalently bound biliverdin (BV) chromophore.
  • It exhibits mild fluorescence and a large Stokes shift, making it a candidate for bioimaging.
  • Current limitations include its tetrameric structure and moderate fluorescence quantum yield.

Purpose of the Study:

  • To investigate the role of biliverdin propionic acid tail protonation states on sandercyanin structure and spectroscopy.
  • To identify key residues involved in oligomerization and their response to chromophore protonation.
  • To provide mechanistic insights for engineering monomeric sandercyanin mutants with enhanced fluorescence for bioimaging.

Main Methods:

  • Utilized a microstate model for biliverdin titration.
  • Employed constant pH molecular dynamics simulations.
  • Analyzed protonation states in apo protein, monomeric mutant, and tetrameric sandercyanin.

Main Results:

  • Identified specific residues potentially mediating oligomerization in response to BV presence and tail protonation.
  • Demonstrated that BV tail protonation impacts chromophore geometry.
  • Observed that absorption properties are less affected by tails compared to fluorescence.

Conclusions:

  • The protonation state of BV propionic tails influences sandercyanin chromophore geometry and likely fluorescence.
  • Specific residues play a crucial role in sandercyanin oligomerization.
  • Understanding these mechanisms is key to engineering improved fluorescent proteins for bioimaging applications.