Utilizing A Novel Technique to Measure Biological Interactions
Poster Number
08B
Format
Poster Presentation
Faculty Mentor Name
Joshua Steimel
Faculty Mentor Department
Mechanical Engineering
Abstract/Artist Statement
There are a large variety of molecular biological interactions that are vital to understand but difficult to quantify. A common example exists in the protein that causes blood clotting. Interactions such as these can occur in a wide range of strengths, speeds, and durations. The nature of these interactions void many measuring techniques of supplying adequate data. ELISA and SPR are some of the most common affinity tests which cannot be used to analyze these interactions. A novel method to better measure these biological interactions has been designed and utilized to measure the affinity of many previously obscure interactions.
The apparatu creates a rotating magnetic field by utilizing a Helmbolt Coils-like system; the difference being that the spacing between the coils are two radii. The current between the coils are controlled via MATLAB and a DAQ. A microscope is focused at the center of the three pairs of coils where a slide containing magnetic particles in a solution is observed.
A ferromagnetic particle can be coated with a ligand and caused to rotate and roll when a rotating magnetic field is present. By using the translation of the rolling particle in a hydrodynamic solution as a baseline, the relative strength of an interaction can be determined by comparing the baseline translation to the translation of a coated particle when a complementary ligand is present on the substrate surface. The difference in the translational distances is due to the differing frictional force caused by the affinity between the ligand coated on the rotating particle and the substrate. By changing the coating ligand and the surface ligand, a variety of biological affinity values can be measured.
Current progress includes determining the baseline affinity values while future work involves determining the affinity values for specific protein interactions.
Location
DeRosa University Center Ballroom
Start Date
27-4-2018 12:30 PM
End Date
27-4-2018 2:30 PM
Utilizing A Novel Technique to Measure Biological Interactions
DeRosa University Center Ballroom
There are a large variety of molecular biological interactions that are vital to understand but difficult to quantify. A common example exists in the protein that causes blood clotting. Interactions such as these can occur in a wide range of strengths, speeds, and durations. The nature of these interactions void many measuring techniques of supplying adequate data. ELISA and SPR are some of the most common affinity tests which cannot be used to analyze these interactions. A novel method to better measure these biological interactions has been designed and utilized to measure the affinity of many previously obscure interactions.
The apparatu creates a rotating magnetic field by utilizing a Helmbolt Coils-like system; the difference being that the spacing between the coils are two radii. The current between the coils are controlled via MATLAB and a DAQ. A microscope is focused at the center of the three pairs of coils where a slide containing magnetic particles in a solution is observed.
A ferromagnetic particle can be coated with a ligand and caused to rotate and roll when a rotating magnetic field is present. By using the translation of the rolling particle in a hydrodynamic solution as a baseline, the relative strength of an interaction can be determined by comparing the baseline translation to the translation of a coated particle when a complementary ligand is present on the substrate surface. The difference in the translational distances is due to the differing frictional force caused by the affinity between the ligand coated on the rotating particle and the substrate. By changing the coating ligand and the surface ligand, a variety of biological affinity values can be measured.
Current progress includes determining the baseline affinity values while future work involves determining the affinity values for specific protein interactions.