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    Fida Biosystems fida software v2.3
    BRICHOS binds to α‐synuclein (αSyn) fibrils but not to αSyn monomers. (a) Flow‐induced dispersion analysis <t>(FIDA)</t> experiments measuring the hydrodynamic radius ( R h ) of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of wildtype (WT) αSyn monomers or WT αSyn fibrils (in monomer concentration equivalents), showing no complex formation of BRICHOS with αSyn monomers but binding to αSyn fibrils. (b) Surface plasmon resonance (SPR) measurements of BRICHOS binding to αSyn fibrils in 20 mM sodium phosphate, 0.2 mM EDTA, pH 7.4, revealing a two‐phase profile with a weak and strong dissociation constant of 350 ± 60 μM and 22 ± 2.0 nM, respectively. (c) FIDA experiments measuring the spike area of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of A53T and A30P αSyn fibrils (in monomer concentration equivalents). (d) Native PAGE analysis of soluble BRICHOS in the presence of WT, A53T, and A30P αSyn fibrils, exhibiting 90.6% ± 4.2%, 95.0% ± 5.5%, and 95.7% ± 1.2%, respectively, of soluble, unbound BRICHOS. The uncropped gels are shown in Figure .
    Fida Software V2.3, supplied by Fida Biosystems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fida+software+v2%2E3/pmc11232276-247-6-9?v=Fida+Biosystems
    Average 90 stars, based on 1 article reviews
    fida software v2.3 - by Bioz Stars, 2026-08
    90/100 stars

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    1) Product Images from "Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS"

    Article Title: Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS

    Journal: Protein Science : A Publication of the Protein Society

    doi: 10.1002/pro.5091

    BRICHOS binds to α‐synuclein (αSyn) fibrils but not to αSyn monomers. (a) Flow‐induced dispersion analysis (FIDA) experiments measuring the hydrodynamic radius ( R h ) of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of wildtype (WT) αSyn monomers or WT αSyn fibrils (in monomer concentration equivalents), showing no complex formation of BRICHOS with αSyn monomers but binding to αSyn fibrils. (b) Surface plasmon resonance (SPR) measurements of BRICHOS binding to αSyn fibrils in 20 mM sodium phosphate, 0.2 mM EDTA, pH 7.4, revealing a two‐phase profile with a weak and strong dissociation constant of 350 ± 60 μM and 22 ± 2.0 nM, respectively. (c) FIDA experiments measuring the spike area of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of A53T and A30P αSyn fibrils (in monomer concentration equivalents). (d) Native PAGE analysis of soluble BRICHOS in the presence of WT, A53T, and A30P αSyn fibrils, exhibiting 90.6% ± 4.2%, 95.0% ± 5.5%, and 95.7% ± 1.2%, respectively, of soluble, unbound BRICHOS. The uncropped gels are shown in Figure .
    Figure Legend Snippet: BRICHOS binds to α‐synuclein (αSyn) fibrils but not to αSyn monomers. (a) Flow‐induced dispersion analysis (FIDA) experiments measuring the hydrodynamic radius ( R h ) of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of wildtype (WT) αSyn monomers or WT αSyn fibrils (in monomer concentration equivalents), showing no complex formation of BRICHOS with αSyn monomers but binding to αSyn fibrils. (b) Surface plasmon resonance (SPR) measurements of BRICHOS binding to αSyn fibrils in 20 mM sodium phosphate, 0.2 mM EDTA, pH 7.4, revealing a two‐phase profile with a weak and strong dissociation constant of 350 ± 60 μM and 22 ± 2.0 nM, respectively. (c) FIDA experiments measuring the spike area of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of A53T and A30P αSyn fibrils (in monomer concentration equivalents). (d) Native PAGE analysis of soluble BRICHOS in the presence of WT, A53T, and A30P αSyn fibrils, exhibiting 90.6% ± 4.2%, 95.0% ± 5.5%, and 95.7% ± 1.2%, respectively, of soluble, unbound BRICHOS. The uncropped gels are shown in Figure .

    Techniques Used: Dispersion, Labeling, Concentration Assay, Binding Assay, SPR Assay, Clear Native PAGE

    BRICHOS binds to α‐synuclein (αSyn) oligomers and reduces their generation by inhibiting secondary nucleation. (a) Rate of formation of new nucleation units from global fit analysis of wildtype αSyn aggregation in the presence of different BRICHOS:αSyn ratios (blue to red color gradient), which is mainly determined by the reduction of secondary nucleation processes by BRICHOS. (b) Estimation of the number of new nucleation units at different BRICHOS:αSyn ratios, showing a substantial decrease in the presence of BRICHOS. (c) Flow‐induced dispersion analysis (FIDA) experiments of hydrodynamic radius ( R h ) of 50 nM BRICHOS‐Alexa 488 in presence of αSyn oligomers (in monomer equivalents), revealing a binding constant of 78.2 ± 1.2 nM.
    Figure Legend Snippet: BRICHOS binds to α‐synuclein (αSyn) oligomers and reduces their generation by inhibiting secondary nucleation. (a) Rate of formation of new nucleation units from global fit analysis of wildtype αSyn aggregation in the presence of different BRICHOS:αSyn ratios (blue to red color gradient), which is mainly determined by the reduction of secondary nucleation processes by BRICHOS. (b) Estimation of the number of new nucleation units at different BRICHOS:αSyn ratios, showing a substantial decrease in the presence of BRICHOS. (c) Flow‐induced dispersion analysis (FIDA) experiments of hydrodynamic radius ( R h ) of 50 nM BRICHOS‐Alexa 488 in presence of αSyn oligomers (in monomer equivalents), revealing a binding constant of 78.2 ± 1.2 nM.

    Techniques Used: Dispersion, Binding Assay



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    fida software v2.3  (Fida Biosystems)
    90
    Fida Biosystems fida software v2.3
    BRICHOS binds to α‐synuclein (αSyn) fibrils but not to αSyn monomers. (a) Flow‐induced dispersion analysis <t>(FIDA)</t> experiments measuring the hydrodynamic radius ( R h ) of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of wildtype (WT) αSyn monomers or WT αSyn fibrils (in monomer concentration equivalents), showing no complex formation of BRICHOS with αSyn monomers but binding to αSyn fibrils. (b) Surface plasmon resonance (SPR) measurements of BRICHOS binding to αSyn fibrils in 20 mM sodium phosphate, 0.2 mM EDTA, pH 7.4, revealing a two‐phase profile with a weak and strong dissociation constant of 350 ± 60 μM and 22 ± 2.0 nM, respectively. (c) FIDA experiments measuring the spike area of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of A53T and A30P αSyn fibrils (in monomer concentration equivalents). (d) Native PAGE analysis of soluble BRICHOS in the presence of WT, A53T, and A30P αSyn fibrils, exhibiting 90.6% ± 4.2%, 95.0% ± 5.5%, and 95.7% ± 1.2%, respectively, of soluble, unbound BRICHOS. The uncropped gels are shown in Figure .
    Fida Software V2.3, supplied by Fida Biosystems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/fida+software+v2%2E3/pmc11232276-247-6-9?v=Fida+Biosystems
    Average 90 stars, based on 1 article reviews
    fida software v2.3 - by Bioz Stars, 2026-08
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    BRICHOS binds to α‐synuclein (αSyn) fibrils but not to αSyn monomers. (a) Flow‐induced dispersion analysis (FIDA) experiments measuring the hydrodynamic radius ( R h ) of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of wildtype (WT) αSyn monomers or WT αSyn fibrils (in monomer concentration equivalents), showing no complex formation of BRICHOS with αSyn monomers but binding to αSyn fibrils. (b) Surface plasmon resonance (SPR) measurements of BRICHOS binding to αSyn fibrils in 20 mM sodium phosphate, 0.2 mM EDTA, pH 7.4, revealing a two‐phase profile with a weak and strong dissociation constant of 350 ± 60 μM and 22 ± 2.0 nM, respectively. (c) FIDA experiments measuring the spike area of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of A53T and A30P αSyn fibrils (in monomer concentration equivalents). (d) Native PAGE analysis of soluble BRICHOS in the presence of WT, A53T, and A30P αSyn fibrils, exhibiting 90.6% ± 4.2%, 95.0% ± 5.5%, and 95.7% ± 1.2%, respectively, of soluble, unbound BRICHOS. The uncropped gels are shown in Figure .

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS

    doi: 10.1002/pro.5091

    Figure Lengend Snippet: BRICHOS binds to α‐synuclein (αSyn) fibrils but not to αSyn monomers. (a) Flow‐induced dispersion analysis (FIDA) experiments measuring the hydrodynamic radius ( R h ) of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of wildtype (WT) αSyn monomers or WT αSyn fibrils (in monomer concentration equivalents), showing no complex formation of BRICHOS with αSyn monomers but binding to αSyn fibrils. (b) Surface plasmon resonance (SPR) measurements of BRICHOS binding to αSyn fibrils in 20 mM sodium phosphate, 0.2 mM EDTA, pH 7.4, revealing a two‐phase profile with a weak and strong dissociation constant of 350 ± 60 μM and 22 ± 2.0 nM, respectively. (c) FIDA experiments measuring the spike area of 50 nM fluorescently labeled BRICHOS‐Alexa 488 in the presence of A53T and A30P αSyn fibrils (in monomer concentration equivalents). (d) Native PAGE analysis of soluble BRICHOS in the presence of WT, A53T, and A30P αSyn fibrils, exhibiting 90.6% ± 4.2%, 95.0% ± 5.5%, and 95.7% ± 1.2%, respectively, of soluble, unbound BRICHOS. The uncropped gels are shown in Figure .

    Article Snippet: The resulting Taylograms were analyzed using FIDA software V2.3 (FIDA Biosystems), which provides a hydrodynamic radius ( R h ) for each binding reaction.

    Techniques: Dispersion, Labeling, Concentration Assay, Binding Assay, SPR Assay, Clear Native PAGE

    BRICHOS binds to α‐synuclein (αSyn) oligomers and reduces their generation by inhibiting secondary nucleation. (a) Rate of formation of new nucleation units from global fit analysis of wildtype αSyn aggregation in the presence of different BRICHOS:αSyn ratios (blue to red color gradient), which is mainly determined by the reduction of secondary nucleation processes by BRICHOS. (b) Estimation of the number of new nucleation units at different BRICHOS:αSyn ratios, showing a substantial decrease in the presence of BRICHOS. (c) Flow‐induced dispersion analysis (FIDA) experiments of hydrodynamic radius ( R h ) of 50 nM BRICHOS‐Alexa 488 in presence of αSyn oligomers (in monomer equivalents), revealing a binding constant of 78.2 ± 1.2 nM.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS

    doi: 10.1002/pro.5091

    Figure Lengend Snippet: BRICHOS binds to α‐synuclein (αSyn) oligomers and reduces their generation by inhibiting secondary nucleation. (a) Rate of formation of new nucleation units from global fit analysis of wildtype αSyn aggregation in the presence of different BRICHOS:αSyn ratios (blue to red color gradient), which is mainly determined by the reduction of secondary nucleation processes by BRICHOS. (b) Estimation of the number of new nucleation units at different BRICHOS:αSyn ratios, showing a substantial decrease in the presence of BRICHOS. (c) Flow‐induced dispersion analysis (FIDA) experiments of hydrodynamic radius ( R h ) of 50 nM BRICHOS‐Alexa 488 in presence of αSyn oligomers (in monomer equivalents), revealing a binding constant of 78.2 ± 1.2 nM.

    Article Snippet: The resulting Taylograms were analyzed using FIDA software V2.3 (FIDA Biosystems), which provides a hydrodynamic radius ( R h ) for each binding reaction.

    Techniques: Dispersion, Binding Assay