Christina Johannsen

• Halvorsen, Trine Grønhaug; Johannsen, Christina & Reubsaet, Leon (2026). Microsampling of proteins from biological matrices: sampling methods and devices, typical workflows, clinical examples, novel applications and innovations. Analytical Methods. ISSN 1759-9660. doi: 10.1039/d6ay00944a. Full text in Research Archive
• Johannsen, Christina; Nguyen, Anna Kha Tu; Shabani, Sasha; Oulie, Inger; Dørum, Siri & Dehnes, Yvette [Show all 8 contributors for this article] (2025). Development of smart samplers and their comparison to dried serum spots for the analysis of growth hormone releasing hormone analogs using LC[sbnd]HRMS/MS. Advances in Sample Preparation. 15. doi: 10.1016/j.sampre.2025.100190. Full text in Research Archive
• Johannsen, Christina; Reubsaet, Leon & Halvorsen, Trine Grønhaug (2024). Revolutionizing biomarker analysis one tip at a time—Coupling antibody to Volumetric Absorptive Microsamplers for sensitive LC-MS analysis. Advances in Sample Preparation. 11. doi: 10.1016/j.sampre.2024.100121. Full text in Research Archive
• Johannsen, Christina; Mrsa, Ago; Halvorsen, Trine Grønhaug & Reubsaet, Leon (2023). Smart sampling as the “Spot-on” Method for LC-MS protein analysis from dried blood spots. Journal of Separation Science. ISSN 1615-9306. 46(18). doi: 10.1002/jssc.202300394. Full text in Research Archive Show summary

  This perspective explores the feasibility of smart sampling with dried blood spots for the determination of proteins and peptides from human biomatrices using liquid chromatography coupled to mass spectrometry for clinical purposes. The focus is on innovative approaches to transform filter paper from a mere sample carrier to an active element in sample preparation, with the aim of reducing the need for extensive and intensive sample preparation in the conventional sense. Specifically, we discuss the use of modified cellulose to integrate sample preparation at an early stage of sample handling. The use of paper immobilized with either trypsin or monoclonal antibodies for protein digestion and affinity clean‐up is discussed as a potential benefit of starting sample preparation instantly at the moment of sampling to optimize time efficiency and enable faster analysis, diagnosis, and follow‐up of patients.

• Johannsen, Christina; Haq, Anam Ul; Reubsaet, Leon & Halvorsen, Trine Grønhaug (2022). On the spot immunocapture in targeted biomarker analysis using paper-bound streptavidin as anchor for biotinylated antibodies. Analytical and Bioanalytical Chemistry. ISSN 1618-2642. 414(19), p. 5979–5989. doi: 10.1007/s00216-022-04161-w. Full text in Research Archive Show summary

  Abstract The modification of an easily available resource like paper to circumvent expensive or intensive sample pretreatment could be the answer to sample analysis in resource-poor regions. Therefore, a novel on-paper device combining sample collection with affinity sample pretreatment is introduced here. Universal smart affinity samplers are produced by a simple KIO 4 -mediated oxidation of cellulose, which functionalizes the paper. This is followed by immobilization of streptavidin. Streptavidin serves as a universal anchor for biotinylated antibodies, enabling simple preparation of tailor-made affinity samplers. The functionality of the device was tested using a model protein (human chorionic gonadotropin, hCG) and biotinylated anti-hCG antibodies for affinity capture. In a laboratory setting, the performance was demonstrated, and a 14-fold increase of target binding compared to binding without bmAb was achieved. The recovery of hCG captured with bmAb-treated samplers was determined to be 33% and comparable to previously described affinity capture approaches. Application of the smart affinity samplers to human serum containing hCG showed an R 2 of 0.98 (200–1000 pg mL −1 ), precision of ≤ 9.1% RSD, and estimated limit of detection of 65 pg mL −1 . Although further optimization and validation are necessary prior to application to real samples in clinical settings, the potential of the device for use in determination of low abundant biomarkers in complex samples has been demonstrated.

• Johannsen, Christina; Koehler, Christian & Thiede, Bernd (2021). Comparison of LFQ and IPTL for Protein Identification and Relative Quantification. Molecules. ISSN 1431-5157. 26(17). doi: 10.3390/molecules26175330. Full text in Research Archive Show summary

  (1) Background: Mass spectrometry-based quantitative proteome profiling is most commonly performed by label-free quantification (LFQ), stable isotopic labeling with amino acids in cell culture (SILAC), and reporter ion-based isobaric labeling methods (TMT and iTRAQ). Isobaric peptide termini labeling (IPTL) was described as an alternative to these methods and is based on crosswise labeling of both peptide termini and MS2 quantification. High quantification accuracy was assumed for IPTL because multiple quantification points are obtained per identified MS2 spectrum. A direct comparison of IPTL with other quantification methods has not been performed yet because IPTL commonly requires digestion with endoproteinase Lys-C. (2) Methods: To enable tryptic digestion of IPTL samples, a novel labeling for IPTL was developed that combines metabolic labeling (Arg-0/Lys-0 and Arg-d4/Lys-d4, respectively) with crosswise N-terminal dimethylation (d4 and d0, respectively). (3) Results: The comparison of IPTL with LFQ revealed significantly more protein identifications for LFQ above homology ion scores but not above identity ion scores. (4) Conclusions: The quantification accuracy was superior for LFQ despite the many quantification points obtained with IPTL.

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