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  1. Article ; Online: Impact of column and stationary phase properties on the productivity in chiral preparative LC.

    Forssén, Patrik / Fornstedt, Torgny

    Journal of separation science

    2018  Volume 41, Issue 6, Page(s) 1346–1354

    Abstract: By generating 1500 random chiral separation systems, assuming two-site Langmuir interactions, we investigated numerically how the maximal productivity ( ... ...

    Abstract By generating 1500 random chiral separation systems, assuming two-site Langmuir interactions, we investigated numerically how the maximal productivity (P
    Language English
    Publishing date 2018-03
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2047990-6
    ISSN 1615-9314 ; 1615-9306
    ISSN (online) 1615-9314
    ISSN 1615-9306
    DOI 10.1002/jssc.201701435
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  2. Article ; Online: Kinetics and interaction studies of anti-tetraspanin antibodies and ICAM-1 with extracellular vesicle subpopulations using continuous flow quartz crystal microbalance biosensor.

    Liangsupree, Thanaporn / Multia, Evgen / Forssén, Patrik / Fornstedt, Torgny / Riekkola, Marja-Liisa

    Biosensors & bioelectronics

    2022  Volume 206, Page(s) 114151

    Abstract: Continuous flow quartz crystal microbalance (QCM) was utilized to study binding kinetics between EV subpopulations (exomere- and exosome-sized EVs) and four affinity ligands: monoclonal antibodies against tetraspanins (anti-CD9, anti-CD63, and anti-CD81) ...

    Abstract Continuous flow quartz crystal microbalance (QCM) was utilized to study binding kinetics between EV subpopulations (exomere- and exosome-sized EVs) and four affinity ligands: monoclonal antibodies against tetraspanins (anti-CD9, anti-CD63, and anti-CD81) and recombinant intercellular adhesion molecule-1 (ICAM-1) or CD54 protein). High purity CD9
    MeSH term(s) Biosensing Techniques ; Extracellular Vesicles/chemistry ; Intercellular Adhesion Molecule-1/analysis ; Intercellular Adhesion Molecule-1/metabolism ; Kinetics ; Quartz Crystal Microbalance Techniques ; Tetraspanins/analysis ; Tetraspanins/metabolism
    Chemical Substances Tetraspanins ; Intercellular Adhesion Molecule-1 (126547-89-5)
    Language English
    Publishing date 2022-03-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 1011023-9
    ISSN 1873-4235 ; 0956-5663
    ISSN (online) 1873-4235
    ISSN 0956-5663
    DOI 10.1016/j.bios.2022.114151
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  3. Article ; Online: Advanced Analysis of Biosensor Data for SARS-CoV-2 RBD and ACE2 Interactions.

    Forssén, Patrik / Samuelsson, Jörgen / Lacki, Karol / Fornstedt, Torgny

    Analytical chemistry

    2020  Volume 92, Issue 17, Page(s) 11520–11524

    Abstract: The traditional approach for analyzing interaction data from biosensors instruments is based on the simplified assumption that also larger biomolecules interactions are homogeneous. It was recently reported that the human receptor angiotensin-converting ... ...

    Abstract The traditional approach for analyzing interaction data from biosensors instruments is based on the simplified assumption that also larger biomolecules interactions are homogeneous. It was recently reported that the human receptor angiotensin-converting enzyme 2 (ACE2) plays a key role for capturing SARS-CoV-2 into the human target body, and binding studies were performed using biosensors techniques based on surface plasmon resonance and bio-layer interferometry. The published affinity constants for the interactions, derived using the traditional approach, described a single interaction between ACE2 and the SARS-CoV-2 receptor binding domain (RBD). We reanalyzed these data sets using our advanced four-step approach based on an adaptive interaction distribution algorithm (AIDA) that accounts for the great complexity of larger biomolecules and gives a two-dimensional distribution of association and dissociation rate constants. Our results showed that in both cases the standard assumption about a single interaction was erroneous, and in one of the cases, the value of the affinity constant
    MeSH term(s) Algorithms ; Angiotensin-Converting Enzyme 2 ; Betacoronavirus/chemistry ; Humans ; Interferometry/statistics & numerical data ; Kinetics ; Ligands ; Peptidyl-Dipeptidase A/chemistry ; Peptidyl-Dipeptidase A/metabolism ; Protein Binding ; Protein Domains ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/metabolism ; Surface Plasmon Resonance/statistics & numerical data
    Chemical Substances Ligands ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Keywords covid19
    Language English
    Publishing date 2020-08-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.0c02475
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  4. Article: Advanced Analysis of Biosensor Data for SARS-CoV-2 RBD and ACE2 Interactions

    Forssén, Patrik / Samuelsson, Jörgen / Lacki, Karol / Fornstedt, Torgny

    Analytical chemistry. 2020 Aug. 10, v. 92, no. 17

    2020  

    Abstract: The traditional approach for analyzing interaction data from biosensors instruments is based on the simplified assumption that also larger biomolecules interactions are homogeneous. It was recently reported that the human receptor angiotensin-converting ... ...

    Abstract The traditional approach for analyzing interaction data from biosensors instruments is based on the simplified assumption that also larger biomolecules interactions are homogeneous. It was recently reported that the human receptor angiotensin-converting enzyme 2 (ACE2) plays a key role for capturing SARS-CoV-2 into the human target body, and binding studies were performed using biosensors techniques based on surface plasmon resonance and bio-layer interferometry. The published affinity constants for the interactions, derived using the traditional approach, described a single interaction between ACE2 and the SARS-CoV-2 receptor binding domain (RBD). We reanalyzed these data sets using our advanced four-step approach based on an adaptive interaction distribution algorithm (AIDA) that accounts for the great complexity of larger biomolecules and gives a two-dimensional distribution of association and dissociation rate constants. Our results showed that in both cases the standard assumption about a single interaction was erroneous, and in one of the cases, the value of the affinity constant KD differed more than 300% between the reported value and our calculation. This information can prove very useful in providing mechanistic information and insights about the mechanism of interactions between ACE2 and SARS-CoV-2 RBD or similar systems.
    Keywords Severe acute respiratory syndrome coronavirus 2 ; algorithms ; analytical chemistry ; biosensors ; dissociation ; humans ; interferometry ; peptidyl-dipeptidase A ; surface plasmon resonance
    Language English
    Dates of publication 2020-0810
    Size p. 11520-11524.
    Publishing place American Chemical Society
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.0c02475
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  5. Article ; Online: Advanced Analysis of Biosensor Data for SARS-CoV-2 RBD and ACE2 Interactions

    Forssén, Patrik / Samuelsson, Jörgen / Lacki, Karol / Fornstedt, Torgny

    Analytical Chemistry

    2020  Volume 92, Issue 17, Page(s) 11520–11524

    Keywords Analytical Chemistry ; covid19
    Language English
    Publisher American Chemical Society (ACS)
    Publishing country us
    Document type Article ; Online
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.0c02475
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  6. Article ; Online: Biosensor-Enabled Deconvolution of the Avidity-Induced Affinity Enhancement for the SARS-CoV-2 Spike Protein and ACE2 Interaction.

    Gutgsell, Aspen Rene / Gunnarsson, Anders / Forssén, Patrik / Gordon, Euan / Fornstedt, Torgny / Geschwindner, Stefan

    Analytical chemistry

    2021  Volume 94, Issue 2, Page(s) 1187–1194

    Abstract: Avidity is an effective and frequent phenomenon employed by nature to achieve extremely high-affinity interactions. As more drug discovery efforts aim to disrupt protein-protein interactions, it is becoming increasingly common to encounter systems that ... ...

    Abstract Avidity is an effective and frequent phenomenon employed by nature to achieve extremely high-affinity interactions. As more drug discovery efforts aim to disrupt protein-protein interactions, it is becoming increasingly common to encounter systems that utilize avidity effects and to study these systems using surface-based technologies, such as surface plasmon resonance (SPR) or biolayer interferometry. However, heterogeneity introduced from multivalent binding interactions complicates the analysis of the resulting sensorgram. A frequently applied practice is to fit the data based on a 1:1 binding model, and if the fit does not describe the data adequately, then the experimental setup is changed to favor a 1:1 binding interaction. This reductionistic approach is informative but not always biologically relevant. Therefore, we aimed to develop an SPR-based assay that would reduce the heterogeneity to enable the determination of the kinetic rate constants for multivalent binding interactions using the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein and the human receptor angiotensin-converting enzyme 2 (ACE2) as a model system. We employed a combinatorial approach to generate a sensor surface that could distinguish between monovalent and multivalent interactions. Using advanced data analysis algorithms to analyze the resulting sensorgrams, we found that controlling the surface heterogeneity enabled the deconvolution of the avidity-induced affinity enhancement for the SARS-CoV-2 spike protein and ACE2 interaction.
    MeSH term(s) Angiotensin-Converting Enzyme 2 ; COVID-19 ; Humans ; Protein Binding ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/metabolism ; Surface Plasmon Resonance
    Chemical Substances Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2021-12-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.1c04372
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  7. Article: Kinetics and interaction studies of anti-tetraspanin antibodies and ICAM-1 with extracellular vesicle subpopulations using continuous flow quartz crystal microbalance biosensor

    Liangsupree, Thanaporn / Multia, Evgen / Forssén, Patrik / Fornstedt, Torgny / Riekkola, Marja-Liisa

    Biosensors & bioelectronics. 2022 June 15, v. 206

    2022  

    Abstract: Continuous flow quartz crystal microbalance (QCM) was utilized to study binding kinetics between EV subpopulations (exomere- and exosome-sized EVs) and four affinity ligands: monoclonal antibodies against tetraspanins (anti-CD9, anti-CD63, and anti-CD81) ...

    Abstract Continuous flow quartz crystal microbalance (QCM) was utilized to study binding kinetics between EV subpopulations (exomere- and exosome-sized EVs) and four affinity ligands: monoclonal antibodies against tetraspanins (anti-CD9, anti-CD63, and anti-CD81) and recombinant intercellular adhesion molecule-1 (ICAM-1) or CD54 protein). High purity CD9⁺, CD63⁺, and CD81⁺ EV subpopulations of <50 nm exomeres and 50–80 nm exosomes were isolated and fractionated using our recently developed on-line coupled immunoaffinity chromatography – asymmetric flow field-flow fractionation system. Adaptive Interaction Distribution Algorithm (AIDA), specifically designed for the analysis of complex biological interactions, was used with a four-step procedure for reliable estimation of the degree of heterogeneity in rate constant distributions. Interactions between exomere-sized EVs and anti-tetraspanin antibodies demonstrated two interaction sites with comparable binding kinetics and estimated dissociation constants Kd ranging from nM to fM. Exomeres exhibited slightly higher affinity compared to exosomes. The highest affinity with anti-tetraspanin antibodies was achieved with CD63⁺ EVs. The interaction of EV subpopulations with ICAM-1 involved in cell internalization of EVs was also investigated. EV – ICAM-1 interaction was also of high affinity (nM to pM range) with overall lower affinity compared to the interactions of anti-tetraspanin antibodies and EVs. Our findings proved that QCM is a valuable label-free tool for kinetic studies with limited sample concentration, and that advanced algorithms, such as AIDA, are crucial for proper determination of kinetic heterogeneity. To the best of our knowledge, this is the first kinetic study on the interaction between plasma-derived EV subpopulations and anti-tetraspanin antibodies and ICAM-1.
    Keywords algorithms ; biosensors ; dissociation ; exosomes ; fractionation ; immunoaffinity chromatography ; intercellular adhesion molecule-1 ; ligands ; quartz crystal microbalance
    Language English
    Dates of publication 2022-0615
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 1011023-9
    ISSN 1873-4235 ; 0956-5663
    ISSN (online) 1873-4235
    ISSN 0956-5663
    DOI 10.1016/j.bios.2022.114151
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  8. Article ; Online: A model free method for estimation of complicated adsorption isotherms in liquid chromatography.

    Forssén, Patrik / Fornstedt, Torgny

    Journal of chromatography. A

    2015  Volume 1409, Page(s) 108–115

    Abstract: Here we show that even extremely small variations in the adsorption isotherm can have a tremendous effect on the shape of the overloaded elution profiles and that the earlier in the adsorption isotherms the variation take place, the larger its impact on ... ...

    Abstract Here we show that even extremely small variations in the adsorption isotherm can have a tremendous effect on the shape of the overloaded elution profiles and that the earlier in the adsorption isotherms the variation take place, the larger its impact on the shape of the elution profile. These variations are so small that they can be "hidden" by the discretization and in the general experimental noise when using traditional experimental methods, such as frontal analysis, to measure adsorption isotherms. But as the effects of these variations are more clearly visible in the elution profiles, the Inverse Method (IM) of adsorption isotherm estimation is an option. However, IM usually requires that one selects an adsorption isotherm model prior to the estimation process. Here we show that even complicated models might not be able to estimate the adsorption isotherms with multiple inflection points that small variations might give rise to. We therefore developed a modified IM that, instead of fixed adsorption isotherm models, uses monotone piecewise interpolation. We first validated the method with synthetic data and showed that it can be used to estimate an adsorption isotherm, which accurately predicts an extremely "strange" elution profile. For this case it was impossible to estimate the adsorption isotherm using IM with a fixed adsorption model. Finally, we will give an example of a real chromatographic system where adsorption isotherm with inflection points is estimated by the modified IM.
    MeSH term(s) Adsorption ; Chromatography, Liquid/methods ; Models, Theoretical ; Thermodynamics
    Language English
    Publishing date 2015-08-28
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1171488-8
    ISSN 1873-3778 ; 0021-9673
    ISSN (online) 1873-3778
    ISSN 0021-9673
    DOI 10.1016/j.chroma.2015.07.030
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  9. Article: Advanced Analysis of Biosensor Data for SARS-CoV-2 RBD and ACE2 Interactions

    Forssén, Patrik / Samuelsson, Jörgen / Lacki, Karol / Fornstedt, Torgny

    Anal Chem

    Abstract: The traditional approach for analyzing interaction data from biosensors instruments is based on the simplified assumption that also larger biomolecules interactions are homogeneous. It was recently reported that the human receptor angiotensin-converting ... ...

    Abstract The traditional approach for analyzing interaction data from biosensors instruments is based on the simplified assumption that also larger biomolecules interactions are homogeneous. It was recently reported that the human receptor angiotensin-converting enzyme 2 (ACE2) plays a key role for capturing SARS-CoV-2 into the human target body, and binding studies were performed using biosensors techniques based on surface plasmon resonance and bio-layer interferometry. The published affinity constants for the interactions, derived using the traditional approach, described a single interaction between ACE2 and the SARS-CoV-2 receptor binding domain (RBD). We reanalyzed these data sets using our advanced four-step approach based on an adaptive interaction distribution algorithm (AIDA) that accounts for the great complexity of larger biomolecules and gives a two-dimensional distribution of association and dissociation rate constants. Our results showed that in both cases the standard assumption about a single interaction was erroneous, and in one of the cases, the value of the affinity constant KD differed more than 300% between the reported value and our calculation. This information can prove very useful in providing mechanistic information and insights about the mechanism of interactions between ACE2 and SARS-CoV-2 RBD or similar systems.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #713341
    Database COVID19

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  10. Article ; Online: Systematic investigations of peak distortions due to additives in supercritical fluid chromatography.

    Glenne, Emelie / Samuelsson, Jörgen / Leek, Hanna / Forssén, Patrik / Klarqvist, Magnus / Fornstedt, Torgny

    Journal of chromatography. A

    2020  Volume 1621, Page(s) 461048

    Abstract: The impact of eluent components added to improve separation performance in supercritical fluid chromatography was systematically, and fundamentally, investigated. The model system comprised basic pharmaceuticals as solutes and eluents containing an amine ...

    Abstract The impact of eluent components added to improve separation performance in supercritical fluid chromatography was systematically, and fundamentally, investigated. The model system comprised basic pharmaceuticals as solutes and eluents containing an amine (i.e., triethylamine, diethylamine, or isopropylamine) as additive with MeOH as the co-solvent. First, an analytical-scale study was performed, systematically investigating the impact of the additives/co-solvent on solute peak shapes and retentions, using a design of experiments approach; here, the total additive concentration in the eluent ranged between 0.021 and 0.105 % (v/v) and the MeOH fraction in the eluent between 16 and 26 % (v/v). The co-solvent fraction was found to be the most efficient tool for adjusting retentions, whereas the additive fraction was the prime tool for improving column efficiency and peak analytical performance. Next, the impacts of the amine additives on the shapes of the so-called overloaded solute elution profiles were investigated. Two principal types of preparative peak deformations appeared and were investigated in depth, analyzed using computer simulation with mechanistic modeling. The first type of deformation was due to the solute eluting too close to the additive perturbation peak, resulting in severe peak deformation caused by co-elution. The second type of deformation was also due to additive-solute interactions, but here the amine additives acted as kosmotropic agents, promoting the multilayer adsorption to the stationary phase of solutes with bulkier aryl groups.
    MeSH term(s) Adsorption ; Chromatography, Supercritical Fluid/methods ; Computer Simulation ; Diethylamines/chemistry ; Ethylamines/chemistry ; Propylamines/chemistry ; Solvents/chemistry
    Chemical Substances Diethylamines ; Ethylamines ; Propylamines ; Solvents ; diethylamine (B035PIS86W) ; 2-propylamine (P8W26T4MTD) ; triethylamine (VOU728O6AY)
    Language English
    Publishing date 2020-03-16
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1171488-8
    ISSN 1873-3778 ; 0021-9673
    ISSN (online) 1873-3778
    ISSN 0021-9673
    DOI 10.1016/j.chroma.2020.461048
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