Automated Circular Dichroism (ACD)

New applications for automated Circular Dichroism spectroscopy

Applied Photophysics has now launched the Chirascan™-plus Automated Circular Dichroism (ACD) spectrometer which enables rapid and accurate analysis combining simultaneous circular dichroism, absorbance and fluorescence detection. The new Chirascan™-plus ACD can be used in a multitude of applications (e.g. biocomparability, forced protein degradation, protein folding, batch-batch analysis, buffer formulations and many more).

 

Typical applications include:

  • Formulations
  • Biosimilarity
  • Drug Discovery
  • Protein Engineering

Optimising biotherapeutic formulations

Used as a label free stability-indicating assay, Chirascan™-plus ACD can identify good formulation candidates earlier for further downstream processing.  By culling formulations that are likely to fail early and focusing on those that are more viable for real time and accelerated stability studies, users can make savings in both time and money.

Combining the label-free and information-rich technique of dynamic multimode spectroscopy (DMS) with the productivity of automation gives a whole new approach to establishing conformational stability under different formulation conditions. The conformational integrity of biotherapeutics as a function of more than one stress condition (e.g. T, pH, ionic strength) is readily determined in unattended operation.

 

Statistical comparison of similar proteins (Biosimilarity)

Research into biosimilar pharmaceutical products has grown exponentially over the last 7 years turning it into a multi-billion pound business. Structure, biological activity and stability are just a few of the complex studies required and, traditionally, these use multiple techniques which are very time consuming and labour intensive.

Automation lends itself to measuring samples repeatedly and thus to generating statistical comparisons. To answer the question: ‘Are these two CD spectra the same?’ is no longer a matter of guesswork – a statistical significance can be associated with the measurements and a quantitative judgment about similarity or otherwise can be made.

 

Drug Discovery

Fast determination of protein characteristics is key to any drug discovery department in pharmaceutical research. Applied Photophysics offers a unique solution providing simultaneous circular dichroism, absorbance and fluorescence measurements in a single, easy to use, automated experiment.

The ACD spectrometer can provide structural, functional, thermodynamic and aggregation data. By automating our system we provide unparalleled productivity, low sample volumes and no human error reducing the pressure on analytical labs and enabling them to focus on discovery.

 

Protein Engineering

Monoclonal antibodies, antibody-like proteins, and other biotherapeutics represent a large and growing number of molecular entities entering human clinical trials in virtually all disease indications. The long-term stability of these potential therapeutics is of crucial importance for their development to drug products. 

The ACD spectrometer provides rapid, accurate, and easy to perform measurement of the thermal melting (Tm) points, which has proven to be an exceptionally good indicator of the relative stability of engineered proteins. 

 

To view an abstract from an application note, please click on Application Notes in the Related Pages menu on the right.

 

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Strategies to compare far-UV Circular Dichroism spectra of similar proteins using Chirascan™-plus Automated Circular Dichroism

Automated titration of bovine serum albumin (BSA) in a phosphate-citrate buffer system

Screening optimal buffer conditions for a therapeutic antibody using Chirascan™-plus Automated Circular Dichroism

Sampling accuracy and reproducibility of the Chirascan™-plus automated CD (ACD) spectrometer

Automated sampling of protein solutions and measurement of their circular dichroism signatures in the far-UV using Chirascan™-plus automated CD (ACD)

A powerful tool for establishing conformational stability of cloned proteins

Optimisation of protein formulation