John E. Baatz, Ph.D.


Associate Professor, Pediatrics
Department of Biochemistry and Molecular Biology, MUSC
 

Ph.D., University of Cincinnati


 baatzje@musc.edu

Dr. Baatz talks with colleagues
Research:
Lung biochemistry. We examine the antimicrobial activity of surfactant protein SP-B and its potential utility for eliminating bacterial infections in human and potentially dolphin lungs. SP-B is a unique protein naturally found in pulmonary surfactant that lines the human lung and aids in the prevention of lung collapse. In addition to this surface-active activity, SP-B also has characteristics similar to other known bactericidal peptides. We are currently examining samples from dolphins in an effort to determine if the surfactant proteins SP-B and SP-C are present in the dolphin lung. If they are present, they may be involved in innate immunity in the dolphin lung. This project seeks to determine 1) the effectiveness of SP-B and specific SP-B peptides for killing a range of bacteria which colonize in the lung in a variety of diseases, 2) if and when degradation of SP-B occurs in diseased states, and 3) the specific areas of the lung in which SP-B is localized and therefore which areas of the lung SP-B could protect from bacterial infection.
An additional area of research focuses on the marine mammal lung proteome as an indicator of the effects of environmental and marine-borne toxins on lung health. This is an exciting untapped field of study and has direct impacts on human lung health since humans share the often-polluted coastal waters, whether by recreation or work related, with dolphins, whales and manatees. This project utilizes proteomic techniques in an effort to identify proteins that are altered in expression or secretion as a result of toxin exposure. 

Dr. Baatz with Kelli at Student Research Day

 Publications:

Dluhy, RA, Shanmukh, S Leapard, JB, Kruger, P, Baatz, JE. Deacylated pulmonary surfactant protein SP-C transforms from a-helical to amyloid fibril structure via a pH-dependent mechanism. An IR Structural Investigation. Biophysical Journal, 2003 (in press).

 Krüger P, Baatz JE, Dluhy RA, Lösche, M. Effect of hydrophobic surfactant protein SP–C on binary phospholipid monolayers. Molecular machinery at the air/water interface. Biophysical Chemistry, 2002; 99(3): 209-22.

 Shanmukh S, Howell P, Baatz JE, Dluhy RA. Effect of Hydrophobic Surfactant Proteins SP-B and SP-C on Phospholipid Monolayers. III. Protein Structure Studied Using 2D IR and βν Correlation Analysis. Biophysical Journal, 2002; 83: 2126-2141.