Title

Utilizing A Novel Technique to Measure Biological Interactions

Poster Number

08B

Lead Author Major

Mechanical Engineering

Lead Author Status

Senior

Format

Poster Presentation

Faculty Mentor Name

Joshua Steimel

Faculty Mentor Email

jsteimel@pacific.edu

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

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Apr 27th, 12:30 PM Apr 27th, 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.