Monday, June 20, 2016

Kulim Kht MPSPR 220A Bionavis

220A NAALI

MP-SPR Navi™ 220A NAALI enables all the measurements as traditional
SPR and moreover, provides premium quality data with PureKinetics™.
It also allows measurements of conformation changes.

Kulim Kht MPSPR 210A Bionavis..


210A VASA

Wider inner diameter of the flow-cell tubings
and 6-sample automation make MP-SPR Navi™
210A VASA ideal for material characterization
and nanoparticle research.

Kulim Kht BioNavis 670nm & 785nm waveguide



From tradition SPR to MP-SPR:
From measurements to understanding
Surface Plasmon Resonance (SPR) is an established method for
biomolecular interaction analysis. It is popular due to its sensitivity
as well as its capability to measure label-free and in real-time.
Multi-Parametric Surface Plasmon Resonance (MP-SPR) is based on
SPR principle, however its advantageous optical setup measures
a full SPR curve which enables new insight into interactions.
For instance, PureKinetics™ feature provides measurements of
small molecules, lipids and biomaterials without bulk effect.
MP-SPR widens the application range of traditional SPR from small
molecules up to nanoparticles and even living cells. Measurements
can be performed also in complex media such as serum.
Additionaly, MP-SPR provides information about layer properties.
Thickness and refractive index (RI) data can be utilized in material
characterization from Ångström thick layers up to micrometers
or to ensure conformation of the molecules on the surface.

Premium quality kinetic data with
PureKinetics™
Bulk effect (sometimes called DMSO effect, salt or solvent artifact) is
the difference in liquid composition between samples and running
buffer. The composition difference is seen as a change in refractive
index, which in turn appears as a shift in measured SPR curve.
In traditional SPR, imaging SPR or localized SPR, only part of the SPR
curve can be seen and therefore, several steps have to be taken in
order to separate true molecular binding from the undesired bulk
effect.
The unique optical setup of MP-SPR instruments enables
cross-correlation of parameters provided by the MP-SPR method
and allows simple in-line elimination of interfering bulk signal
using PureKinetics™ feature. This feature is available in all
MP-SPR Navi™ instruments.

Kulim Kht Nanoparticle with MPSPR BioNavis


Gold nanoparticles were immobilized on a monolayer selfassembled
on gold. Functional groups on the chain ends of the
monolayer facilitated an anchoring of gold nanoparticles to the
layer. Multi-Parametric Surface Plasmon Resonance (MP-SPR)
enabled a real-time measurement of the binding of the gold
nanoparticles to the surface layer.
Introduction
Gold nanoparticles (AuNPs) exhibits interesting optical and electronic
properties that find application in sensors, catalysis, electronics,
photonics, solar cells, cancer diagnosis and therapy. Controlled attachment
of Au nanoparticles at a solid interface is required for many of
these applications. Although many methods have been developed to
fabricate Au nanoparticle assemblies, developing simple and effective
routes is still very attractive. Usually, the immobilization can be
performed using a covalent or an electrostatic interaction between
the nanoparticles and the substrate. In this study functional molecules
are used for linking gold nanoparticles to a solid surface. Molecules
possessing functional groups can be attached to the solid surface in
a controlled manner and permits nanoparticle immobilization.

Conclusions
Monolayers with functional groups assembled on a gold surface
can be used for coupling of gold nanoparticles. In this study MP-SPR
turned out to be a unique method for determining the deposition of
metal nanoparticles to the surface layer in real-time. AuNPs exhibit
strong surface plasmon resonances and even a large response could
be observed by MP-SPR when nanoparticles were interacting with
the surface layer. Functional groups on the chains ends enable
an anchoring of gold nanoparticles or even embedding into the
chains. MP-SPR is a unique tool for studying metal nanoparticles for
applications in sensors, electronics, photonics, solar cells or cancer
diagnosis and therapy.

Kulim Kht Pure Kinetic with MPSPR Bionavis


When is the PureKinetics™ useful?
• with Kinetic measurements of small molecules
• with Interaction measurements on lipid bilayers
• when there are Material interactions with biomolecules
• in case of Solvent interactions
• when using Crude samples (serum, growth medium, lysate, seawater)

IgG dissociation kinetics from immobilized Protein A was
studied using real-time Multi-Parametric Surface Plasmon
Resonance (MP-SPR). Various dissociation buffers were
tested to determine the most efficient solution. A unique
feature, PureKinetics™, allows differentiation of real binding
from interfering bulk signal artifacts, providing a pure
binding signal. The method can clear out even extremely
large bulk signals, such as high-ionic strength dissociation
buffers. In this study, the most efficient dissociation from
Protein A was achieved with buffers of pH below 4.0.

Introduction
Surface Plasmon Resonance (SPR) is a well-established method for
molecule-molecule interaction studies. The SPR is a popular real-time
and label-free method measuring association and dissociation kinetic
constants in addition to the affinity constant. Multi-Parametric Surface
Plasmon Resonance (MP-SPR) is based on the SPR principle, but it utilizes
a unique optical setup which allows to solve challenges related to the
buffer composition changes during SPR measurements.
In non-labelled optical methods, changes in buffer composition
frequently cause a shift of the peak minimum angle value due to a
change in refractive index of the buffer (called bulk effect or solvent
effect). The usual method to counteract this is to subtract a reference
channel response from the measurement channel response. However,
the bulk effect is often not exactly the same in the different measurement
channels because ligands might prevent the liquid flow near the
surface. Sometimes suitable reference surface is hard to find, especially
in the case of interactions to a membrane protein or interactions to
coatings. Therefore, better methods than reference channel correction
to compensate for bulk artifacts are needed.
Many small molecule weight drugs have poor solubility in water-based
liquids, and solubility enhancers such as dimethyl-sulfoxide (DMSO) are
needed to obtain suitable solubility. As the organic solubility enhancers
create a large bulk signal in SPR, they also create huge challenges to
assays in terms of a protein stability and function. Traditionally the bulk
effect caused by DMSO is corrected using an empirical calibration curve
requiring multiple injections [Frostell-Karlsson et al. 2000].
The unique optical setup of the MP-SPR instruments enables
measurement of multiple optical parameters simultaneously and in
real-time. Cross-correlation of the parameters allows simple in line
characterization of the interfering bulk signal using the PureKinetics™
feature.