Imperial College London
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DrSarahHedberg

Faculty of Engineering, Department of Chemical Engineering

 
 
 
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Contact

 

+44 (0)20 7594 6227s.hedberg13

 
 
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Location

 

C410Roderic Hill BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@inproceedings{Hedberg:2015,
author = {Hedberg, S and Heng, JYY and Williams, DR and Liddell, J},
pages = {1150--1151},
title = {Chromatographic tools to predict the stability of mAbs for faster identification of therapeutic candidates},
year = {2015}
}
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RIS format (EndNote, RefMan)

TY  - CPAPER
AB  - Protein-protein molecular interactions are known to be involved in protein solution aggregation behaviour and are a common issue for the manufacturing of therapeutic proteins such as mAbs. Much effort has been employed to gain a better understanding of aggregation, however the mechanisms leading to protein aggregation are still not fully understood. The osmotic second virial coefficient (B22) is a fundamental physiochemical property that describes protein-protein interactions solution, which can be a useful tool to predict aggregation propensity of proteins. One way of predicting aggregation propensity is self-interaction chromatography (SIC), which recently have shown to be a promising tool for better understanding of phase behaviour of proteins. Another technique, cross-interaction chromatography (CIC), has shown to be an even more high-throughput technique than its predecessor with possibly the same capabilities. This work consists of two experimental studies with therapeutic mAbs to improve SIC and CIC as a tool to predict protein aggregation. The first part includes a 10 times scale-down study of therapeutic mAbs from laboratory scale macro-columns to micro-scale columns, which will enable the determination of B22 for the individual protein as well as the cross-virial coefficient, B23, between two proteins. Micro SIC and CIC uses only a few milligrams of mAb in order to obtain a complete formulation study. The results from the first part of the study proved to give good comparable results between the micro and macro scales enabling the use of micro SIC for B22 determinations. The second part of this work presents an extensive formulation study of mAbs, varying pH and salt, as well as the presence of different stabilisers as well as different external factors known to induce aggregation. The B22 and B23 values determined from the formulation study are then correlated with aggregation data obtained from size-exclusion chromatography. It was shown that over all te
AU  - Hedberg,S
AU  - Heng,JYY
AU  - Williams,DR
AU  - Liddell,J
EP  - 1151
PY  - 2015///
SP  - 1150
TI  - Chromatographic tools to predict the stability of mAbs for faster identification of therapeutic candidates
ER  -
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