Presentation Title

Using Virus Nanoparticles to Develop an Alternative Antagonist to Heparin

Faculty Mentor

Andrew K. Udit

Start Date

17-11-2018 8:30 AM

End Date

17-11-2018 10:30 AM

Location

CREVELING 44

Session

POSTER 1

Type of Presentation

Poster

Subject Area

biological_agricultural_sciences

Abstract

Heparin is a glucose-based polysaccharide which functions as a clinical anticoagulant. To reverse the effects of heparin, protamine sulfate is currently the only FDA-approved drug available for this role. However, protamine sulfate is known to cause several problems including severe anaphylactic reactions and arterial hypertension. We use the bacteriophage Qβ virus as a platform for displaying cationic groups to bind to and reverse the effects of heparin. A current focus of the project is to determine thermodynamic parameters of interactions between Qβ and heparin and the binding characteristics between Qβ and heparin-coated surfaces. The specific experimental parameters for binding of heparin to Qβ protein are currently being studied using isothermal titration calorimetry (ITC) and biolayer interferometry. Using ITC measures heat changes from the binding of the virus particles and heparin, and calculates the binding constants, number of active sites, enthalpy, and entropy in the reaction while biolayer interferometry measures binding constants between heparin covered surfaces and the virus nanoparticle.

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Nov 17th, 8:30 AM Nov 17th, 10:30 AM

Using Virus Nanoparticles to Develop an Alternative Antagonist to Heparin

CREVELING 44

Heparin is a glucose-based polysaccharide which functions as a clinical anticoagulant. To reverse the effects of heparin, protamine sulfate is currently the only FDA-approved drug available for this role. However, protamine sulfate is known to cause several problems including severe anaphylactic reactions and arterial hypertension. We use the bacteriophage Qβ virus as a platform for displaying cationic groups to bind to and reverse the effects of heparin. A current focus of the project is to determine thermodynamic parameters of interactions between Qβ and heparin and the binding characteristics between Qβ and heparin-coated surfaces. The specific experimental parameters for binding of heparin to Qβ protein are currently being studied using isothermal titration calorimetry (ITC) and biolayer interferometry. Using ITC measures heat changes from the binding of the virus particles and heparin, and calculates the binding constants, number of active sites, enthalpy, and entropy in the reaction while biolayer interferometry measures binding constants between heparin covered surfaces and the virus nanoparticle.