Elizabeth R. Gaillard
Transmission of Light to the Young Primate Retina: Possible Implications for the Formation of Lipofuscin. Gaillard, E.R.; Merriam, J.; Zheng, L.; Dillon, J. (2011) Photochem. Photobiol., 87: 18–21.
Compositional Studies of Human RPE Lipofuscin: mechanisms of molecular modifications. Murdaugh, L.S.; Mandal, S.; Dillon, J.; Simon, J.D.; Gaillard, E.R. (2011) J. Mass Spectrom., 46: 90–95.
Compositional Studies of Human RPE Lipofuscin. Murdaugh, L.S.; Avalle, L.B.; Mandal, S.; Dillon, J.; Simon, J.D.; Gaillard, E.R. (2010) J. Mass Spectrom., 45: 1139–1147.
Carborane‐Appended C3‐Symmetrical Extended π‐Systems: Synthesis and Properties. Hosmane, N.; Dash, B.; Satapathy, R.; Gaillard, E.R.; Maguire, J. (2010) J. Am. Chem. Soc., 132: 6578–6587.
Age‐Related Accumulation of 3‐nitrotyrosine and nitro‐A2E in Human Bruch's Membrane. Murdaugh, L.S.; Wang, Z.; Del Priore, L.V.; Dillon, J.; Gaillard, E.R. (2010) Exp. Eye Res., 90: 564–571.
Physical Properties of the Lipid Bilayer Membrane made of Cortical and Nuclear Bovine Lens Lipids: EPR Spin‐Labeling Studies. Raguz, M.; Widomska, J.; Dillon, J.; Gaillard, E.R.; Subczynski, W.K. (2009) Biochem Biophys Acta, 1788: 2380–2388.
Modifications to the basement membrane protein, laminin, by glycolaldehyde and A2E: model system for age related changes to Bruch's membrane. Murdaugh, L.; Dillon, J.; Gaillard, E.R. (2009) Exp. Eye Res., 89: 187–192.
Isolation and characterization of a spontaneously immortalized bovine retinal pigmented epithelium cell line. Liggett, T.E.; Griffiths, T.D.; Gaillard, E.R. (2009) BMC Cell Biology, (doi:10.1186/1471‐2121‐10‐33).
Characterization of lipid domains in reconstituted porcine lens membranes using EPR spin labeling approaches. Gaillard, E.R.; Subczynski, W.K. (2008) Biochem. Biophys. Acta, 1778: 1079–1090.
Light Damage in Biological Tissues
The general topic of interest in our research group is the study of the mechanisms involved in photooxidative damage to biological systems, particularly in the human eye. Photooxidative damage is implicated in a number of ocular disorders such as age‐related cataract formation and age‐related macular degeneration (AMD; the leading cause of blindness in older adults). Light damage to biological systems may not manifest itself on a macroscopic level for decades, but the damage is initiated by short‐lived, electronically excited species that participate in Type I or Type II oxidative chemistry. We use a wide variety of experimental methods to study these systems, including laser‐based time‐resolved spectroscopy. By determining the sequence of events that leads to tissue injury and identifying the reactive species along the reaction pathway, we may be able to develop methods to slow down or stop these processes.
Currently, we are pursuing three major projects:
- In collaboration with several other research groups, we have developed new methods for accurately measuring the absorption/transmission properties of the individual ocular components, as well as the collective spectra of the anterior segment of the eye. These studies are important because they allow us to define exactly what portion and what intensity of the ambient spectrum is transmitted to each structure.
- Several retinal disorders, most notably AMD, are associated with the accumulation of lipofuscin, a mixture of pigments, in the retinal pigment epithelium. Lipofuscin absorbs visible light that is transmitted to the retina; it has also been observed to sensitize singlet oxygen in vitro. We are investigating the photochemistry of several components of lipofuscin to determine their potential role in enhancing oxidative stress in the retina. These studies also have potential applications to non‐invasive diagnostic methods.
- One age‐related change that occurs in the human lens is the gradual yellowing of the lens proteins. The lens consists of a highly concentrated protein solution, as well as several chromophores of low molecular weight that absorb light that is transmitted through the cornea. We are developing model systems for the yellowed lens proteins by photochemically attaching the native chromophores to lens protein and then comparing their photochemical properties to those of isolated human lens proteins.
Research Fellow, Center for Photoinduced Charge Transfer, 1995–1996
Research Fellow, Center for Fast Kinetics Research, 1992–1994
Visiting Assistant Professor, Southwest Texas State University, 1991–1992
Ph.D., University of Texas at Austin, 1991
B.S., Florida State University, 1984
Photochemistry, chemical kinetics, time‐resolved spectroscopy, photooxidative damage to biological tissue.