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Biacore Facility Core

Director: Cohen, Gary., PhD


Biacore units use Surface Plasmon Resonance (SPR), enabling investigators to detect and monitor biomolecular binding events in real-time. This allows the user to gain a better understanding of biochemical mechanisms associated with protein-ligand interactions. The Penn Dental Medicine Biacore Facility Core features two Biacore units – the Biacore X and the Biacore 3000. The Biacore X is a manually operated unit with two flow cells, and the Biacore 3000 is a fully automated unit with four flow cells and multiple capabilities.
SPR is a valuable research tool to assay components by defining their interactions, providing quantitative information on:
-- Specificity – how specific is the binding between two molecules?
-- Concentration – how much of given molecule is present and active?
-- Kinetics – what is the rate of association/dissociation?
-- Affinity – how strong is the binding?

A special unit installed into the Biacore 3000 is an SPR–MALDI interface block. The block is designed to recover molecules that bind to a protein fixed to the sensor surface in the small volumes that are suitable for mass spectrometry. Bound component(s) are eluted into the micro-recovery module and analyzed by mass spectrometry, which identifies the bound component(s). This has been used to:
-- Characterize native or recombinant protein-protein and protein-ligand interactions.
-- Characterize antibodies by determining competition groups, affinity of binding, and ability to bind to various forms of a protein.
-- Characterize potential drug targets or diagnostic markers.



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Last updated: 2019-12-13T09:24:00.111-05:00

Copyright © 2016 by the President and Fellows of Harvard College
The eagle-i Consortium is supported by NIH Grant #5U24RR029825-02 / Copyright 2016