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Northern Illinois University

Chemistry & Biochemistry

Professor Elizabeth R. Gaillard

(Joint appointment in the Department of Biological Sciences)

Elizabeth R. Gaillard

Associate Professor
Office:  Faraday West 322
Phone:  (815) 753-6908
gaillard@niu.edu

 



Educational Background

Ph.D., University of Texas at Austin, 1991

B.S., Florida State University, 1984

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

Curriculum Vitae (pdf)

Research Interests

Photochemistry, chemical kinetics, time-resolved spectroscopy, photooxidative damage to biological tissue.

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Representative Publications

Structure prediction of the RPE65 protein. Guo, H.; Zheng, C.; Gaillard, E. R. (2006) J. Theor. Biol., in press.

Antioxidant properties of melanin in RPE cells. Wang, Z.; Dillon, J.; Gaillard, E. R. (2006) Photochem. Photobiol., 82: 474–479.

Action spectrum for singlet oxygen production by human retinal lipofuscin. Avalle, L. B.; Dillon, J.; Gaillard, E. R. (2005) Photochem. Photobiol., 81: 1347-1350.

Non-enzymatic nitration of extracellular matrix proteins deleteriously affects retinal pigment epithelial cell function and viability: A comparison study with non-enzymatic glycation mechanisms. Wang, Z.; Paik, D. C.; del Priore, L. V.; Gaillard, E. R. (2005) Curr. Eye Res., 30: 691-702.

A mechanistic study of the photooxidation of A2E, a component of human retinal lipofuscin. Gaillard, E. R.; Avalle, L. B.; Keller, L. M. M.; Wang, Z.; Reszka, K.; Dillon, J. (2004) Exp. Eye Res., 79: 313-319.

The photochemical oxidation of A2E results in the formation of a 5,8,5’,8’-bisfuranoid oxide. Dillon, J.; Wang, Z.; Avalle, L. B.; Gaillard, E. R. (2004) Exp. Eye Res., 79: 537-542.

In vivo measurement of time resolved auto-fluorescence at the human ocular fundus. Schweitzer, D.; Hammer, M.; Schweitzer, F.; Anders, R.; Doebbecke, T.; Schenke, S.; Gaillard, E. R. (2004) J. Biomed. Optics, 9: 1214-1222.

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.


Laser-Based Flash Photolysis System

The laser-based flash photolysis system we use in my research group.


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.