Zetasizer Nano ZSP: A Perfect Tool For Life Science Applications

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1 Zetasizer Nano ZSP: A Perfect Tool For Life Science Applications Dr Mike Kaszuba Technical Support Manager michael.kaszuba@malvern.com Contents Zetasizer Nano ZSP Software Enhancements Protein Applications Protein Mobility 1

2 Contents Zetasizer Nano ZSP Software Enhancements Protein Applications Protein Mobility Zetasizer Nano ZSP A high specification Zetasizer Nano with enhanced sensitivity and two new measurement types Microrheology Protein Mobility 2

3 What is New in the Zetasizer Nano ZSP? Improved zeta potential sensitivity Especially applicable to nanoparticles and biomolecules Enables better measurement of protein mobility and charge Protein mobility measurement type New measurement type for measurements of protein electrophoretic mobility Automates process of protein mobility measurements Assesses quality of protein mobility measurements DLS microrheology option Rheological characterization of low viscosity, weakly-structured samples Very small sample volumes Applications for viscosity of polymer and protein solutions and onset of protein aggregation Software additions and extended protein utilities New suite of calculators Protein charge calculation Sensitivity of the Zetasizer Nano ZSP Optical enhancements Increased laser power (1mW) Redesigned detection optics Higher sensitivity NIBS count-rate doubled Forward angle size sensitivity increased >1 fold Zeta Potential sensitivity increased >1 fold Measurement of protein mobility (zeta potential) at concentrations down to 1mg/ml 3

4 Protein Mobility Measurements Superior protein mobility measurements in three parts: 1) High sensitivity system Zetasizer Nano ZSP 2) Protect the sample from the electrodes Diffusion Barrier Method (low sample volume 2 to 1µL) 3) Appropriate measurement parameters Protein mobility measurement type Electrophoretic Mobility of BSA at 1mg/mL Stability of protein mobility mean using diffusion barrier method ±.91 µmcm/vs sets of 5 measurements -1 show the same results Mobility (µmcm/vs) Record number Mean protein mobility (mean ± SD) (µmcm/vs) ± ± ± ±.383 Average mobility ±.91 Mobility (µmcm/vs) Record Index Record Index 4

5 Primary Application for the ZSP Protein zeta potential or, more accurately Protein electrophoretic mobility Derive protein charge Calculated from mobility measurements Faster and more convenient than existing methods such as capillary electrophoresis and iso-electric focussing Application - protein therapeutics Effect of charge on the catalytic effect of protein activity Reaction kinetics Binding of protein and substrates Monitoring protein denaturing Contents Zetasizer Nano ZSP Software Enhancements Protein Applications Protein Mobility 5

6 Protein Utility Calculators DLS Debye Plot DLS interaction parameter, k D (for protein interactions) True hydrodynamic radius (R h= at concentration k D DLS Interaction Parameter Where; D m = mutual (measured) diffusion coefficient D = self diffusion coefficient (diffusion coefficient at C = ) C = sample concentration Yadav, S. et. al. (212) J. Pharm. Sci. 11,

7 Protein Utility Calculators Protein charge and f(κa) Calculate protein apparent charge from measured electrophoretic mobility Also calculates f(κa) for the Henry equation to improve zeta potential calculation Other Protein Utility Calculators Interparticle distance Determines distance between molecules and electrical double layer dimensions Virial diameter Calculates the effective molecular or collision diameter (thermodynamic diameter) Mixture Viscosity Estimates the effective viscosity for a mixture of dispersants Oligomer ratios Estimates mass proportions of a protein monomer/dimer mixture where the size of each is known User selectable solvent layer thickness in shape estimates Improves accuracy of quoted protein size 7

8 Molecular Weight Measurements The molecular weight measurement process has been improved so that measurements can be made across different attenuators It is possible to measure down to attenuator 7 Can now measure count rate over a much wider range Approximatly 8x increase in count rate range Measure derived count rate up to 4, kcps More reliable values of Mw and A 2 KC/RoP (1/kDa) Concentration (g/ml) Corrected Scattering (kcps) Protein Melting Point Aggregation Point This is a more appropriate name with respect to what the Zetasizer actually measures The algorithm for calculating the aggregation point has been significantly improved to make it more reliable 8

9 Other Software Improvements Modified workspaces and minor report improvements Easier to export correlation function and size distributions Contents Zetasizer Nano ZSP Software Enhancements Protein Applications Protein Mobility 9

10 Why are Protein Interactions Important? Biopharmaceuticals are a growing family of drugs where the active ingredient is a protein Protein chemists are increasingly trying to predict and understand protein behaviour in drug formulations It is desirable to make biopharmaceuticals at high concentrations so to reduce dosing size and frequency but this can result in high viscosity and aggregation A growing body of evidence is showing that protein mobility, A 2 and k D can all help to understand and predict this behaviour Protein Mobility There is growing recognition that protein electrophoretic mobility is an important value to understand Since buffer conditions are high variable, it is more appropriate to talk about protein electrophoretic mobility than zeta potential Effective protein charge can be calculated from the protein mobility Using the new protein charge calculator in the Zetasizer software 1

11 Protein Mobility Measurement Type The protein mobility measurement combines three features to maximise measurement quality The protein mobility measurement combines size and zeta measurements (at the same measurement angle) to see that no protein aggregates are forming during the measurement Mobility measurements are performed in groups of sub-runs to allow for periods of cooling to reduce the chance of aggregation through heating Automated optimisation reduces the voltage based on sample conductivity to further reduce the risk of aggregation Protein Mobility Sequence Automated Measurement Optimization Measure Size Measure Mobility Measure Size Group 1 Pause Group 2 Pause Group 3 Sun run 1 Sub run 2 Sub run 3 Sub run 4 Etc Etc 11

12 Protein Mobility Results Protein mobility results take the form of a parent/child structure Results are displayed in the Protein Mobility workspace Human Serum Albumin Mobility at ph 7 Intensity (Percent) Size (d.nm) Pure protein at beginning Size measured to be 3.8 nm Good mobility measurement Almost as pure at end Measured mobility -.88 µmcm/vs Calculated charge Total Counts 2 1 Intensity (Percent) Frequency (Hz) Size (d.nm) 12

13 Human Serum Albumin Mobility at ph 4 Intensity (Percent) Size (d.nm) Pure protein at beginning Size measured to be 4.1 nm Good mobility measurement Almost as pure at end Measured mobility.44 µmcm/vs Calculated charge +7 Total Counts Intensity (Percent) Frequency (Hz) Size (d.nm) Assessing Protein Interactions Light scattering is increasingly being used to monitor protein interactions Two parameters that are becoming more widely used are the second virial coefficient (A 2 ) and the DLS interaction parameter (k D ) A Dynamic Debye Plot looks at measured diffusion coefficient as a function of protein concentration The dynamic virial coefficient (k D ) is calculated from this plot 13

14 Measurements of A 2 HSA A 2 becomes more positive with a ph change from ph 4 to 7 ph 4 ph 7 Measurements of k D HSA k D becomes more positive with a ph change from ph 4 to 7 ph 4 ph 7 14

15 HSA Behaviour Summary Between ph 7 and ph 4 Size increases slightly Mobility becomes more positive A 2 and k D tend towards zero Protein rate of aggregation over time increases significantly HSA ph 7 ph 4 Hydrodynamic radius (nm) Mobility (µmcm/vs) A 2 (ml mol/g 2 ) 1.93 x x 1-5 k D (ml/g) Rate of aggregation Slow Fast 15

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