Quantification of Alefacept, an immunosuppressive fusion protein in human plasma using a protein analogue internal standard, trypsin cleaved signature peptides and liquid chromatography tandem mass spectrometry

Halquist, Matthew S.; Karnes, H. Thomas

doi:10.1016/j.jchromb.2011.02.034

Cited by 25 publications

(14 citation statements)

References 38 publications

(49 reference statements)

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“…Partial protein precipitation, using organic solvents along with surfactants, is used as a simple sample purification technique to deplete the endogenous plasma proteins. Partial protein precipitation eliminates larger proteins but leave smaller ones in solution [11][12][13]. Protein precipitation could have low recovery due to losses as a result co-precipitation, which would be a drawback.…”

Section: Non-selective Protein Enrichment Techniquesmentioning

confidence: 99%

“…Halquist et al reported an LC-MS/MS method for quantification of Alefacept, a therapeutic protein for treatment of psoriasis, in human plasma using horse heart myoglobin a protein analogue internal standard [11]. The method used partial protein precipitation to selectively precipitate background proteins while retaining the analyte protein and the internal standard protein in solution.…”

Section: Analogue Proteins As Internal Standardsmentioning

confidence: 99%

“…Eight internal standardization approaches were compared with respect to accuracy and precision in work flows with and without digestion. Both analogue IS standard proteins (eel and human calcitonin), SIL-salmon calcitonin, SIL-salmon calcitonin signature peptide [1][2][3][4][5][6][7][8][9][10][11], and the cleavable SIL-salmon calcitonin peptide [1][2][3][4][5][6][7][8][9][10][11] were commercially obtained. 18 O-labeled form of the signature peptide was synthesized in-house by isotope exchange with18 O-labeled water.…”

Section: Comparison Of Protein Sil-is Versus Peptides Ismentioning

confidence: 99%

“…Besides human calcitonin (added before and after digestion), all other approaches tested in workflow B, including the omission of an internal standard, generated acceptable results, which shows that in this workflow all steps were well under control. Again, the best results in terms of precision and accuracy were obtained when SIL-salmon calcitonin , cleavable SIL peptide internal standard and SIL peptide [1][2][3][4][5][6][7][8][9][10][11] were used as internal standards. Since there was no difference between the performance of a SIL-calcitonin, cleavable SIL-peptide and that of a SIL-peptide for workflow B, it was concluded that the digestion step did not negatively impact method performance.…”

Section: Comparison Of Protein Sil-is Versus Peptides Ismentioning

confidence: 99%

See 3 more Smart Citations

Internal Standards for Absolute Quantification of Large Molecules (Proteins) from Biological Matrices by LC-MS/MS

Faria¹,

Halquist²

2018

Calibration and Validation of Analytical Methods - A Sampling of Current Approaches

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Internal standardization plays a critical role in the performance of a bioanalytical method. There has been a tremendous increase in the popularity of using liquid chromatography tandem mass spectrometry (LC-MS/MS) methods for quantitative bioanalysis of protein molecules. Protein, being too large to be directly analyzed by LC-MS/MS, is proteolyzed and a characteristic peptide is used as a surrogate analyte for quantification. Internal standardization in small molecules' analysis is straightforward, i.e., either a stable labeled isotope (SIL) form of the analyte or a structural analogue is used. As protein quantification involves protein digestion to yield peptides, there are more options for internal standardization. Currently, internal standard selection is based on the availability of the internal standards and the sample preparation workflow. A SIL-form of the analyte protein is the ideal internal standard. However, its use is limited due to cost and commercial availability. Alternatively, a SIL form the surrogate peptide analyte or a cleavable SIL-peptide can be used as an IS. For preclinical bioanalysis of humanized IgG antibody-based drugs, a universal SIL analogue protein has been effectively used as an internal standard. This chapter focuses on internal standardization for the quantitative analysis of proteins, such as biotherapeutics and biomarkers, using LC-MS/MS.

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Section: Non-selective Protein Enrichment Techniquesmentioning

confidence: 99%

Section: Analogue Proteins As Internal Standardsmentioning

confidence: 99%

Section: Comparison Of Protein Sil-is Versus Peptides Ismentioning

confidence: 99%

Section: Comparison Of Protein Sil-is Versus Peptides Ismentioning

confidence: 99%

See 2 more Smart Citations

Internal Standards for Absolute Quantification of Large Molecules (Proteins) from Biological Matrices by LC-MS/MS

Faria¹,

Halquist²

2018

Calibration and Validation of Analytical Methods - A Sampling of Current Approaches

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View full text Add to dashboard Cite

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“…Our previous successes with column trapping lead us to investigate 2D-LC for chromatographic separation of OXM. Initially, C18 guard columns were attempted as the loading column to provide a short loading time as demonstrated previously [36]. The mobile phase optimization study of 3-NBA described in Section 2.5 provided compelling evidence to continue use of the Waters XBridge BEH300 C18 for the analytical column.…”

Section: D-lc-ms/ms Using Reversed Phase Ion Pair Chromatographymentioning

confidence: 99%

Determination of oxyntomodulin, an anorectic polypeptide, in rat plasma using 2D-LC–MS/MS coupled with ion pair chromatography

Halquist

Sakagami

Karnes

2012

Journal of Chromatography B

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LC/MSversus Immune‐Based Bioanalytical Methods in Quantitation of Therapeutic Biologics in Biological Matrices

Zhang

2015

Pharmaceutical Sciences Encyclopedia

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This chapter reviews the main characteristics of liquid chromatography/mass spectrometry (LC/MS) and ligand‐binding assay (LBA) methods. If an LBA method for biotherapeutics quantification is well established, it usually provides sufficient sensitivity and selectivity and is considered the method of choice. The LC/MS method emerged as an alternative strategy for quantification of proteins of interest in complex biological matrices. Multiplexed capacity and selectivity are critical features determining the applicability of a bioanalytical method. Well‐established LBA methods usually provide adequate sensitivity for quantification analysis of biotherapeutics in preclinical/clinical pharmacokinetic (PK)/pharmacodynamic (PD) study. LC/MS with high resolution analyzer has become a promising technology for characterization of antibody‐drug conjugate (ADC) in the recent years. An affinity capture capillary LC coupled to quadrupole‐time‐of‐flight (TOF) MS has been employed to analyze anti‐MUC16 TDC, which obtained both in vitro and in vivo drug‐to‐antibody ratios (DARs) information.

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Quantification of Alefacept, an immunosuppressive fusion protein in human plasma using a protein analogue internal standard, trypsin cleaved signature peptides and liquid chromatography tandem mass spectrometry

Cited by 25 publications

References 38 publications

Internal Standards for Absolute Quantification of Large Molecules (Proteins) from Biological Matrices by LC-MS/MS

Internal Standards for Absolute Quantification of Large Molecules (Proteins) from Biological Matrices by LC-MS/MS

Determination of oxyntomodulin, an anorectic polypeptide, in rat plasma using 2D-LC–MS/MS coupled with ion pair chromatography

LC/MSversus Immune‐Based Bioanalytical Methods in Quantitation of Therapeutic Biologics in Biological Matrices

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