Office Phone: (210) 458-5694
Areas of Specialization:
Our group investigates various protein/dye systems. The goal is to establish and understand the mechanisms by which photoactive dyes non-covalently attached to proteins can prompt conformational changes of the protein upon irradiation with visible light. These studies are then used to either inactivate
specific proteins or introduce photosensitive, “artificial” properties (structural, enzymatic, etc.) to globular proteins.
We also use the same approach, in conjunction with self-assembly with nanoparticles, to study protein/dye complexes that in aqueous solution would be capable of converting solar energy into molecular hydrogen in a photosynthetic mimic that could be developed for biomolecular fuel cells.
Fernandez, N.F., Sansone, S., Belcher, J., Haskins, W.E., Brancaleon, L., 2009, Photo-induced unfolding of b-lactoglobulin mediated by a water soluble porphyrin. The Journal of Physical Chemistry B. 113:6020-6030.
Renthal, R., Brancaleon, L., Peña, I., Silva, F., Chen, L.Y., 2011, Interaction of a two-transmembrane-helix peptide with lipid bilayers and dodecyl sulfate micelles, Biophysical Chemistry. 159:321-327 doi: 10.1016/j.bpc.2011.08.005.Penick, M.A., Baffoe, D., Smith, T.D., Mahindaratne, M.P.D., Brancaleon, L., Negrete, G.R., 2012, Claisen Rearrangement Route to Novel Electron-Rich Perylene Dyes, Arkivoc, vi:112-118