| 1. |
- Durall, Claudia, et al.
(författare)
-
Robust QCM-Based Sensing and Assay Formats in Commercialized Systems
- 2023
-
Ingår i: Springer Series on Chemical Sensors and Biosensors. - : Springer.
-
Bokkapitel (refereegranskat)abstract
- Attana’s Quartz Crystal Microbalance (QCM) analytical instruments have been developed to study in vitro biological interactions, mimicking the in vivo conditions. Attana’s superior technology for kinetic interaction studies allows to perform different assays, including biochemical, crude, sera, cell, and tissue-based, in vitro diagnostic and material chemistry assays, in real time and label free. With the focus to validate, select, and optimize drug candidates prior to clinical trials, Attana has helped pharmaceutical companies to increase their efficiency and profitability. In addition, the Attana instruments and services have been used in many other applications and research as described in this chapter.
|
|
| 2. |
- Mahajan, Rashmi, et al.
(författare)
-
Oxytocin-Selective Nanogel Antibody Mimics
- 2022
-
Ingår i: International Journal of Molecular Sciences. - : MDPI. - 1661-6596 .- 1422-0067. ; 23:5
-
Tidskriftsartikel (refereegranskat)abstract
- Oxytocin imprinted polymer nanoparticles were synthesized by glass bead supported solid phase synthesis, with NMR and molecular dynamics studies used to investigate monomer-template interactions. The nanoparticles were characterized by dynamic light scattering, scanning- and transmission electron microscopy and X-ray photoelectron spectroscopy. Investigation of nanoparticle-template recognition using quartz crystal microbalance-based studies revealed sub-nanomolar affinity, k(d) approximate to 0.3 +/- 0.02 nM (standard error of the mean), comparable to that of commercial polyclonal antibodies, k(d) approximate to 0.02-0.2 nM.
|
|
| 3. |
- Nilsson, Per H., 1980-, et al.
(författare)
-
Quartz Crystal Microbalance Platform for SARS-CoV-2 Immuno-Diagnostics
- 2023
-
Ingår i: International Journal of Molecular Sciences. - : MDPI. - 1661-6596 .- 1422-0067. ; 24:23
-
Tidskriftsartikel (refereegranskat)abstract
- Rapid and accurate serological analysis of SARS-CoV-2 antibodies is important for assessing immune protection from vaccination or infection of individuals and for projecting virus spread within a population. The quartz crystal microbalance (QCM) is a label-free flow-based sensor platform that offers an opportunity to detect the binding of a fluid-phase ligand to an immobilized target molecule in real time. A QCM-based assay was developed for the detection of SARS-CoV-2 antibody binding and evaluated for assay reproducibility. The assay was cross-compared to the Roche electrochemiluminescence assay (ECLIA) Elecsys (R) Anti-SARS-CoV-2 serology test kit and YHLO's chemiluminescence immunoassay (CLIA). The day-to-day reproducibility of the assay had a correlation of r(2) = 0.99, p < 0.001. The assay linearity was r(2) = 0.96, p < 0.001, for dilution in both serum and buffer. In the cross-comparison analysis of 119 human serum samples, 59 were positive in the Roche, 52 in the YHLO, and 48 in the QCM immunoassay. Despite differences in the detection method and antigen used for antibody capture, there was good coherence between the assays, 80-100% for positive and 96-100% for negative test results. In summation, the QCM-based SARS-CoV-2 IgG immunoassay showed high reproducibility and linearity, along with good coherence with the ELISA-based assays. Still, factors including antibody titer and antigen-binding affinity may differentially affect the various assays' responses.
|
|
| 4. |
- Persson Skare, Tor, et al.
(författare)
-
Quartz Crystal Microbalance Measurement of Histidine-Rich Glycoprotein and Stanniocalcin-2 Binding to Each Other and to Inflammatory Cells
- 2022
-
Ingår i: Cells. - : MDPI. - 2073-4409. ; 11:17
-
Tidskriftsartikel (refereegranskat)abstract
- The plasma protein histidine-rich glycoprotein (HRG) is implicated in the polarization of macrophages to an M1 antitumoral phenotype. The broadly expressed secreted protein stanniocalcin 2 (STC2), also implicated in tumor inflammation, is an HRG interaction partner. With the aim to biochemically characterize the HRG and STC2 complex, binding of recombinant HRG and STC2 preparations to each other and to cells was explored using the quartz crystal microbalance (QCM) methodology. The functionality of recombinant proteins was tested in a phagocytosis assay, where HRG increased phagocytosis by monocytic U937 cells while STC2 suppressed HRG-induced phagocytosis. The binding of HRG to STC2, measured using QCM, showed an affinity between the proteins in the nanomolar range, and both HRG and STC2 bound individually and in combination to vitamin D3-treated, differentiated U937 monocytes. HRG, but not STC2, also bound to formaldehyde-fixed U937 cells irrespective of their differentiation stage in part through the interaction with heparan sulfate. These data show that HRG and STC2 bind to each other as well as to U937 monocytes with high affinity, supporting the relevance of these interactions in monocyte/macrophage polarity.
|
|
