Advisor(s)
Binaya Baral, Gary Lorigan
Confirmation
1
Document Type
Poster
Location
ONU McIntosh Center; Activities Room
Start Date
24-4-2026 12:00 PM
End Date
24-4-2026 12:50 PM
Abstract
The phage protein gp28 is a bacterial membrane lysis protein that functions outside of currently understood canonical pathways for bacterial lysis. Primarily, lysis is done in conjunction with proteins called spanins, however about 15% of gram negative bacteria infecting phages have coding for spanins. This led to the discovery of the disruptins, a class of non-spanin outer membrane disrupting proteins which includes gp28 from the φKT phage. To understand the mechanism in which gp28 disrupts the outer membrane, we employ spin labeling of the protein in its synthesis and create samples of artificial membranes. Using electron paramagnetic resonance (EPR), we are able to detect the binding and affinity of various points in the protein to understand what each section of the protein does.
Recommended Citation
Sutherland, Maxwell; Baral, Binaya; and Lorigan, Gary, "Spin-label Probing of gp28 Elucidates Interactions with Lipid Vesicles using CW-EPR" (2026). ONU Student Research Colloquium. 61.
https://digitalcommons.onu.edu/student_research_colloquium/2026/Posters/61
Spin-label Probing of gp28 Elucidates Interactions with Lipid Vesicles using CW-EPR
ONU McIntosh Center; Activities Room
The phage protein gp28 is a bacterial membrane lysis protein that functions outside of currently understood canonical pathways for bacterial lysis. Primarily, lysis is done in conjunction with proteins called spanins, however about 15% of gram negative bacteria infecting phages have coding for spanins. This led to the discovery of the disruptins, a class of non-spanin outer membrane disrupting proteins which includes gp28 from the φKT phage. To understand the mechanism in which gp28 disrupts the outer membrane, we employ spin labeling of the protein in its synthesis and create samples of artificial membranes. Using electron paramagnetic resonance (EPR), we are able to detect the binding and affinity of various points in the protein to understand what each section of the protein does.