Study the structural effects of maculatin 1.1 on supported lipid bilayers (SLBs) by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0419-WXH)

Introduction

Maculatin 1.1 (Mac1)s is an antimicrobial peptide (AMP) from the skin secretions of the Australian tree frog Litoria genimaculata. The peptide forms part of the frog's innate immune system and is effective at killing a wide range of Gram-positive bacteria. This makes Mac1, along with a range of other AMPs found across nature, a possibility for development of alternative antibiotics. Alternatives are required due to the increasing prevalence of antibiotic resistance by bacteria to the most commonly used antibiotics currently available, making what were once treatable infections increasingly difficult to treat. Mechanistically, what makes most AMPs an attractive target is that they target disrupting the cell membrane rendering the cell unviable and making it improbable for resistance to occur, rather than targeting a metabolic process where bacteria can evolve to develop resistance.

Add to Cart Please Inquire

Principle Applications Procedure Materials Notes Related Products

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 the structural effects of maculatin 1.1 on supported lipid bilayers (SLBs).
Development of alternative antibiotics.

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

Other recommended products

Determination the binding affinity of supported lipid bilayers (SLBs) by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0416-WXH)
Measurement and Differentiation of Ligand-Induced Calmodulin Conformations by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0385-WXH)
Monitoring the prevention of amyloid fibril formation by α-crystallin by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0450-WXH)
Study of Mussel adhesive protein (MAP) on adsorption solid surfaces by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0435-WXH)
Characterize and develop HydroMIP-based protein biosensors by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0451-WXH)
Study of the formation of supported lipid bilayers (SLBs) by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0417-WXH)
Study growth of microtubules on surface by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0449-WXH)
Study of lysozyme on adsorption solid surfaces by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0431-WXH)