Figure 1: The Biacore T100

 


Figure 2: Surface plasmon resonance (SPR) technology detects the change in reflected light angle from the side of the chip opposite of the flow channel according to the mass bound to the surface of the chip.

 


Figure 3: The kinetics of an interaction can be determined from the information in a sensorgram.

 


Biomolecular Interactions with the Biacore T100



The Biacore T100 uses surface plasmon resonance (SPR) technology, to detect Biomolecular interactions in real time and label-free. SPR technology detects the change in reflected light angle from the side of the chip opposite of the flow channel according to the mass bound to the surface of the chip. The advantages of the Biacore T100 are its sensitivity, temperature controls, improved microfluidics and software, and automation.

Pre-Project Evaluation:

To better evaluate how to design your biacore experiment, please download and fill out this pre-project evaluation form and email to biacore_support@ouhsc.edu.

Biacore T100 Applications:
  • yes/no binding
  • affinity
  • binding kinetics
  • thermodynamics
  • multiple binding
  • concentration
Molecules for interactions:
  • Nucleic acid
  • Protein
  • Small molecules
  • Membranes
  • Whole cells or viruses
Sensor Chips:
  • CM5 - carboxymethylated dextran matrix
  •     *Immobilization via -NH2, -SH, -CHO, -OH, or -COOH groups
  • CM4 - Lower degree of carboxymethylation than CM5 (less negatively chardged)
  •     * reduced nonspecific binding
  • CM3 - Shorter carboxymethylated dextran matrix than CM5
  •     * works well with whole cells
  • C1 - Flat carboxymethylated surface, no dextran matrix
  •     *works for attaching cells and viruses
  • NTA - CM5+nitrilotriacetic acid
  •     *Immobilization of his-tagged molecules
  • SA - CM5+streptavidin
  •     *Immobilization of biotinylated peptides, proteins, nucleic acids or carbohydrates
  • HPA - CM5+lypophilic substance
  •     *Immobilization of model membrane systems
  • L1 - Carboxymethylated dextran matrix with lipophilic substaces
  •     *capture of liposomes
Videos:
  • Specificity
  • Kinetics: rates of reaction
  • Affinity: the strength of binding
  • Concentration
  • Multiple interactions during complex formation
  • Using surface plasmon resonance (SPR)
  • Detecting interactions in realtime
  • Biacore Flexchip; a new angle on SPR


Contacts:

E-mail: biacore_support@ouhsc.edu

Phone:
Dr. Allison Gillaspy: 405-271-2337 ext. 1