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Study of Membrane-Lytic Peptides by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0398-WXH)

Introduction

A wide range of antimicrobial peptides act via binding to and subsequent disruption of cell membranes. A number of different mechanisms have been proposed to describe the mode of action of these peptides. These models vary from general bilayer disruption following the binding of a critical concentration of peptide, the formation of pores, or through the binding with specific lipophilic components of the membrane such as lipopolysaccharides.




Principle

Dual polarization interferometry (DPI) is an analytical technique that allows the simultaneous determination of thickness, density, and mass of a biological layer on a sensing waveguide surface in real time. DPI focuses laser light into two waveguides. One of these functions as the "sensing" waveguide having an exposed surface while the second one functions to maintain a reference beam. A two-dimensional interference pattern is formed in the far field by combining the light passing through the two waveguides. The DPI technique rotates the polarization of the laser, to alternately excite two polarization modes of the waveguides. Measurement of the interferogram for both polarizations allows both the refractive index and the thickness of the adsorbed layer to be calculated. These measurements can be used to infer conformational information about the molecular interactions taking place, as the molecule size (from the layer thickness) and the fold density (from the RI) change.

Applications

Study of Membrane-Lytic Peptides

Procedure

1. Setting of dual polarization interferometry
2. Preparing the DPI sensor chip
3. Immobilization of target on DPI biosensor
4. Reagent was injected to react
5. Quantitative analysis

Materials

• DPI biosensor
• DPI sensor chip
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