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Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Reference Protocol to Assess Analytical Performance of Higher Order Structural Analysis Measurements
T2 - Results from an Interlaboratory Comparison
AU - Groves, K.
AU - Ashcroft, A.E.
AU - Cryar, A.
AU - Sula, A.
AU - Wallace, B.A.
AU - Stocks, B.B.
AU - Burns, C.
AU - Cooper-Shepherd, D.
AU - De Lorenzi, E.
AU - Rodriguez, E.
AU - Zhang, H.
AU - Ault, J.R.
AU - Ferguson, J.
AU - Phillips, J.J.
AU - Pacholarz, K.
AU - Thalassinos, K.
AU - Luckau, L.
AU - Ashton, L.
AU - Durrant, O.
AU - Barran, P.
AU - Dalby, P.
AU - Vicedo, P.
AU - Colombo, R.
AU - Davis, R.
AU - Parakra, R.
AU - Upton, R.
AU - Hill, S.
AU - Wood, V.
AU - Soloviev, Z.
AU - Quaglia, M.
PY - 2021/7/6
Y1 - 2021/7/6
N2 - Measurements of protein higher order structure (HOS) provide important information on stability, potency, efficacy, immunogenicity, and biosimilarity of biopharmaceuticals, with a significant number of techniques and methods available to perform these measurements. The comparison of the analytical performance of HOS methods and the standardization of the results is, however, not a trivial task, due to the lack of reference protocols and reference measurement procedures. Here, we developed a protocol to structurally alter and compare samples of somatropin, a recombinant biotherapeutic, and describe the results obtained by using a number of techniques, methods and in different laboratories. This, with the final aim to provide tools and generate a pool of data to compare and benchmark analytical platforms and define method sensitivity to structural changes. Changes in somatropin HOS, induced by the presence of zinc at increasing concentrations, were observed, both globally and at more localized resolution, across many of the methods utilized in this study and with different sensitivities, suggesting the suitability of the protocol to improve understanding of inter- and cross-platform measurement comparability and assess analytical performance as appropriate. © 2021 The Authors. Published by American Chemical Society.
AB - Measurements of protein higher order structure (HOS) provide important information on stability, potency, efficacy, immunogenicity, and biosimilarity of biopharmaceuticals, with a significant number of techniques and methods available to perform these measurements. The comparison of the analytical performance of HOS methods and the standardization of the results is, however, not a trivial task, due to the lack of reference protocols and reference measurement procedures. Here, we developed a protocol to structurally alter and compare samples of somatropin, a recombinant biotherapeutic, and describe the results obtained by using a number of techniques, methods and in different laboratories. This, with the final aim to provide tools and generate a pool of data to compare and benchmark analytical platforms and define method sensitivity to structural changes. Changes in somatropin HOS, induced by the presence of zinc at increasing concentrations, were observed, both globally and at more localized resolution, across many of the methods utilized in this study and with different sensitivities, suggesting the suitability of the protocol to improve understanding of inter- and cross-platform measurement comparability and assess analytical performance as appropriate. © 2021 The Authors. Published by American Chemical Society.
KW - Chemical analysis
KW - Analytical performance
KW - Biopharmaceuticals
KW - Higher-order structure
KW - Interlaboratory comparison
KW - Measurement comparability
KW - Measurements of
KW - Reference measurements
KW - Reference protocols
KW - Chemistry
U2 - 10.1021/acs.analchem.0c04625
DO - 10.1021/acs.analchem.0c04625
M3 - Journal article
VL - 93
SP - 9041
EP - 9048
JO - Analytical Chemistry
JF - Analytical Chemistry
SN - 0003-2700
IS - 26
ER -