Comparison of predicted extinction coefficients of monoclonal antibodies with experimental values as measured by the Edelhoch method

Maity, Haripada; Wei, Anji; Chen, Ethan; Haidar, Jaafar N.; Srivastava, Arvind K.; Goldstein, J.

doi:10.1016/j.ijbiomac.2015.03.027

Cited by 17 publications

(5 citation statements)

References 22 publications

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“…1b), where the molar extinction coefficients of antibody, Alexa 488, and ICG are 216 000 M À1 cm À1 (at 280 nm), 71 000 M À1 cm À1 (at 495 nm), and 147 000 M À1 cm À1 (at 800 nm), respectively. 28,29 The labelling efficiency was 50% for Alexa 488-Herceptin and 89% for ICG-Herceptin conjugates. For other antibody conjugates, the labelling efficiencies of the Alexa 488 and ICG dye were summarized in Fig.…”

Section: Resultsmentioning

confidence: 98%

Shortwave-infrared (SWIR) fluorescence molecular imaging using indocyanine green–antibody conjugates for the optical diagnostics of cancerous tumours

Tsuboi

2020

RSC Adv.

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Section: Resultsmentioning

confidence: 98%

Shortwave-infrared (SWIR) fluorescence molecular imaging using indocyanine green–antibody conjugates for the optical diagnostics of cancerous tumours

Tsuboi

2020

RSC Adv.

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“…no scatter or luminescence correction). It should be noted, however, that the D320 has been reported as a means to correct for scattering at 280 nm [ 18 ]. Proteins absorb little to no light at 320 nm, and therefore the D320 represents scattered rather than absorbed light.…”

Section: Resultsmentioning

confidence: 99%

The NISTmAb Reference Material 8671 value assignment, homogeneity, and stability

et al. 2018

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The NISTmAb Reference Material (RM) 8671 is intended to be an industry standard monoclonal antibody for pre-competitive harmonization of best practices and designing next generation characterization technologies for identity, quality, and stability testing. It must therefore embody the quality and characteristics of a typical biopharmaceutical product and be available long-term in a stable format with consistent product quality attributes. A stratified sampling and analysis plan using a series of qualified analytical and biophysical methods is described that assures RM 8671 meets these criteria. Results for the first three lots of RM 8671 highlight the consistency of material attributes with respect to size, charge, and identity. RM 8671 was verified to be homogeneous both within and between vialing lots, demonstrating the robustness of the lifecycle management plan. It was analyzed in concert with the in-house primary sample 8670 (PS 8670) to provide a historical link to this seminal material. RM 8671 was verified to be fit for its intended purpose as a technology innovation tool, external system suitability control, and cross-industry harmonization platform. Graphical abstractThe NISTmAb Reference Material (RM) 8671 is intended to be an industry standard monoclonal antibody for pre-competitive harmonization of best practices and designing next generation characterization technologies for identity, quality, and stability testing. Electronic supplementary materialThe online version of this article (10.1007/s00216-017-0800-1) contains supplementary material, which is available to authorized users.

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“…The latter differs from one mAb to another regarding their number of tyrosine and tryptophan residues according to the Edelhoch or Pace equation [23]. The difference of the extinction coefficient between mAbs, differing by their composition on ArA, has been demonstrated experimentally by Maity et al [33]. Global conformation of the protein (native/unfolded), the location of the ArA particularly in the Fv fragments, the solvation of the mAb, and the π cation interactions between the alkali ion and aromatic residues (and lysine or arginine residues) are also parameters that influence the mAb extinction coefficient.…”

Section: Second-derivative Spectramentioning

confidence: 94%

High-throughput identification of monoclonal antibodies after compounding by UV spectroscopy coupled to chemometrics analysis

et al. 2016

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Monoclonal antibodies (mAbs) compounded into the hospital pharmacy are widely used nowadays. Their fast identification after compounding and just before administration to the patient is of paramount importance for quality control at the hospital. This remains challenging due to the high similarity of the structure between mAbs. Analysis of the ultraviolet spectral data of four monoclonal antibodies (cetuximab, rituximab, bevacizumab, and trastuzumab) using unsupervised principal component analysis led us to focus exclusively on the second-derivative spectra. Partial least squares-discriminant analysis (PLS-DA) applied to these data allowed us to build models for predicting which monoclonal antibody was present in a given infusion bag. The calibration of the models was obtained from a k-fold validation. A prediction set from another batch was used to demonstrate the ability of the models to predict well. PLS-DA models performed on the spectra of the region of aromatic amino acid residues presented high ability to predict mAb identity. The region corresponding to the tyrosine residue reached the highest score of good classification with 89 %. To improve the score, standard normal variate (SNV) preprocessing was applied to the spectral data. The quality of the optimized PLS-DA models was enhanced and the region from the tyrosine/tryptophan residues allowed us excellent classification (100 %) of the four mAbs according to the matrix of confusion. The sensitivity and specificity performance parameters assessed this excellent classification. The usefulness of the combination of UV second-derivative spectroscopy to multivariate analysis with SNV preprocessing demonstrated the unambiguous identification of commercially available monoclonal antibodies. Graphical abstract PLS-DA models on the spectra of the region of aromatic amino acid residues allows mAb identification with high prediction.

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Comparison of predicted extinction coefficients of monoclonal antibodies with experimental values as measured by the Edelhoch method

Cited by 17 publications

References 22 publications

Shortwave-infrared (SWIR) fluorescence molecular imaging using indocyanine green–antibody conjugates for the optical diagnostics of cancerous tumours

Shortwave-infrared (SWIR) fluorescence molecular imaging using indocyanine green–antibody conjugates for the optical diagnostics of cancerous tumours

The NISTmAb Reference Material 8671 value assignment, homogeneity, and stability

High-throughput identification of monoclonal antibodies after compounding by UV spectroscopy coupled to chemometrics analysis

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