Nine surface plasmon resonance assays for specific protein quantitation during cell culture and process development

Frostell, Åsa; Mattsson, Anna; Eriksson, Åsa; Wallby, Elisabeth; Kärnhall, Johan; Illarionova, N. B.; Nilsson, Camilla

doi:10.1016/j.ab.2015.02.010

Cited by 7 publications

(6 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous studies compared time of complete SPR and ELISA analysis and showed that SPR measurements can determine 100 samples in 16 h, with hands‐on time of approximately 1 h and automated analysis overnight. In contrast to this, ELISA was performed in this study for IgA and IgGsc with a total time of analysis of 10 samples in 6 h each, with hands‐on time of approximately 4 h. . Although, automated microfluidic ELISA systems have been shown to decrease assay time to 30 min .…”

Section: Discussionmentioning

confidence: 99%

“…In general, it is possible to use a functionalized sensor surface over a period of one month and over 1000 binding cycles can be conducted, respectively (unpublished data, Bruker Daltonics SPR). Other systems can compensate reasonable changes in surface activity using calibration trend functionality (Biacore T200) and have shown reusability of the same immobilized surface for approximately 250 binding cycles during a time period of 12 days .…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Monitoring bioactive and total antibody concentrations for continuous process control by surface plasmon resonance spectroscopy

Zschätzsch

Ritter

Henseleit

et al. 2019

Engineering in Life Sciences

View full text Add to dashboard Cite

Monoclonal antibodies have become an increasingly important part of fundamental research and medical applications. To meet the high market demand for monoclonal antibodies in the biopharmaceutical sector, industrial manufacturing needs to be achieved by large scale, highly productive and consistent production processes. These are subject to international guidelines and have to be monitored intensely due to high safety standards for medical applications. Surface plasmon resonance spectroscopy — a fast, real‐time, and label‐free bio‐sensing method — represents an interesting alternative to the quantification of monoclonal antibody concentrations by enzyme‐linked immunosorbent assay during monoclonal antibody production. For the application of monitoring bioactive and total monoclonal antibody concentrations in cell culture samples, a surface plasmon resonance assay using a target‐monoclonal antibody model system was developed. In order to ensure the subsequent detection of bioactive monoclonal antibody concentrations, suitable immobilization strategies of the target were identified. A significant decrease of the limit of detection was achieved by using an adapted affinity method compared to the commonly used amine coupling. Furthermore, the system showed limit of detection in the low ng/mL range similar to control quantifications by enzyme‐linked immunosorbent assay. Moreover, the comparison of total to bioactive monoclonal antibody concentrations allows analysis of antibody production efficiency. The development of an alternative quantification system to monitor monoclonal antibody production was accomplished using surface plasmon resonance with the advantage of low analyte volume, shorter assay time, and biosensor reusability by target‐layer regeneration. The established method provides the basis for the technical development of a surface plasmon resonance‐based system for continuous process monitoring.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Monitoring bioactive and total antibody concentrations for continuous process control by surface plasmon resonance spectroscopy

Zschätzsch

Ritter

Henseleit

et al. 2019

Engineering in Life Sciences

View full text Add to dashboard Cite

show abstract

“…Under conditions of mass transport limitations, such a graph should be linear, with a null initial value [32,34], although a four-parameter logistic function has also been used [65,95], allowing a broader applicability, since the linearity range may be limited. Rather than the slope, some authors used the SPR signal obtained at the end of a set analyte injection time as the measurement, which may have a broader applicability outside the linearity range [58,65,66,69].…”

Section: Spr To Measure Concentrationsmentioning

confidence: 99%

“…Surface plasmon resonance-based biosensors represent an interesting option in that regard, as they can be used to quantify the product (as a faster alternative to ELISA) and to probe binding to its biological partners, which can often be indicative of the product quality, efficacy, and/or safety. SPR has been used to analyze various types of molecules in this context, including antibodies [65][66][67]102], fusion proteins [57], peptides [68], complement fragments [58], and other blood proteins [66,103].…”

Section: Spr Applications To Biotherapeutics Production Monitoringmentioning

confidence: 99%

“…A concentration analysis is also possible [32][33][34][35], and as such, SPR represents an interesting alternative to enzyme-linked immunosorbent assays (ELISA) for quantitation purposes [36]. SPR technology has been used in multiple fields, such as drug screening [16][17][18]21]; drug potency assessments [37]; vaccine quantitation [38][39][40][41][42]; food safety (the detection of bacteria, pathogens, and other impurities) [43][44][45][46][47][48][49][50]; biotherapeutics characterization and quality control [51][52][53][54][55][56][57]; biotherapeutic safety [58]; medical diagnostics [20,[59][60][61][62][63]; environmental monitoring [64]; and bioproduction monitoring [55,[65][66][67][68]. Although little work has been done for the aim of using an SPR biosensor online or at-line from a bioreactor in an automatic fashion [67,…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

On the Use of Surface Plasmon Resonance-Based Biosensors for Advanced Bioprocess Monitoring

et al. 2021

View full text Add to dashboard Cite

Biomanufacturers are being incited by regulatory agencies to transition from a quality by testing framework, where they extensively test their product after their production, to more of a quality by design or even quality by control framework. This requires powerful analytical tools and sensors enabling measurements of key process variables and/or product quality attributes during production, preferably in an online manner. As such, the demand for monitoring technologies is rapidly growing. In this context, we believe surface plasmon resonance (SPR)-based biosensors can play a role in enabling the development of improved bioprocess monitoring and control strategies. The SPR technique has been profusely used to probe the binding behavior of a solution species with a sensor surface-immobilized partner in an investigative context, but its ability to detect binding in real-time and without a label has been exploited for monitoring purposes and is promising for the near future. In this review, we examine applications of SPR that are or could be related to bioprocess monitoring in three spheres: biotherapeutics production monitoring, vaccine monitoring, and bacteria and contaminant detection. These applications mainly exploit SPR’s ability to measure solution species concentrations, but performing kinetic analyses is also possible and could prove useful for product quality assessments. We follow with a discussion on the limitations of SPR in a monitoring role and how recent advances in hardware and SPR response modeling could counter them. Mainly, throughput limitations can be addressed by multi-detection spot instruments, and nonspecific binding effects can be alleviated by new antifouling materials. A plethora of methods are available for cell growth and metabolism monitoring, but product monitoring is performed mainly a posteriori. SPR-based biosensors exhibit potential as product monitoring tools from early production to the end of downstream processing, paving the way for more efficient production control. However, more work needs to be done to facilitate or eliminate the need for sample preprocessing and to optimize the experimental protocols.

show abstract

A universal SI-traceable isotope dilution mass spectrometry method for protein quantitation in a matrix by tandem mass tag technology

Jin

et al. 2016

Anal Bioanal Chem

View full text Add to dashboard Cite

Isotope dilution mass spectrometry (IDMS), an important metrological method, is widely used for absolute quantification of peptides and proteins. IDMS employs an isotope-labeled peptide or protein as an internal standard although the use of a protein provides improved accuracy. Generally, the isotope-labeled protein is obtained by stable isotope labeling by amino acids in cell culture (SILAC) technology. However, SILAC is expensive, laborious, and time-consuming. To overcome these drawbacks, a novel universal SI-traceable IDMS method for absolute quantification of proteins in a matrix is described with human transferrin (hTRF). The hTRF and a human serum sample were labeled with different tandem mass tags (TMTs). After mixing the TMT-labeled hTRF and serum sample together followed by digestion, the peptides were separated by nano-liquid chromatography and analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Using the signature peptides, we calculated the ratios of reporter ions from the TMT-labeled peptides which, in turn, allowed determination of the mass fraction of hTRF. The recovery ranged from 97% to 105% with a CV of 3.9%. The LOD and LOQ were 1.71 × 10(-5) g/g and 5.69 × 10(-5) g/g of hTRF in human serum, respectively, and the relative expanded uncertainty was 4.7% with a mass fraction of 2.08 mg/g. For comparison, an enzyme-linked immunosorbent assay (ELISA) method for hTRF yielded a mass fraction of 2.03 mg/g. This method provides a starting point for establishing IDMS technology to accurately determine the mass fractions of protein biomarkers in a matrix with traceability to SI units. This technology should support the development of a metrological method useful for quantification of a wide variety of proteins.

show abstract

Nine surface plasmon resonance assays for specific protein quantitation during cell culture and process development

Cited by 7 publications

References 14 publications

Monitoring bioactive and total antibody concentrations for continuous process control by surface plasmon resonance spectroscopy

Monitoring bioactive and total antibody concentrations for continuous process control by surface plasmon resonance spectroscopy

On the Use of Surface Plasmon Resonance-Based Biosensors for Advanced Bioprocess Monitoring

A universal SI-traceable isotope dilution mass spectrometry method for protein quantitation in a matrix by tandem mass tag technology

Contact Info

Product

Resources

About