j 1100 circular dichroism spectrometer  (JASCO Inc)


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    JASCO Inc j 1100 circular dichroism spectrometer
    J 1100 Circular Dichroism Spectrometer, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    j 1100 circular dichroism spectrometer  (JASCO Inc)


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    JASCO Inc j 1100 circular dichroism spectrometer
    J 1100 Circular Dichroism Spectrometer, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    j 1100 model spectrometer  (JASCO Inc)


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    JASCO Inc j 1100 model spectrometer
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    j 1100 cd spectrophotometer  (JASCO Inc)


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    JASCO Inc j 1100 cd spectrophotometer
    J 1100 Cd Spectrophotometer, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    j 1100 spectropolarimeter  (JASCO Inc)


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    JASCO Inc j 1100 spectropolarimeter
    PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system <t>(J-1100,</t> JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.
    J 1100 Spectropolarimeter, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Direct disassembly of α-syn preformed fibrils into native α-syn monomers by an all-D-peptide"

    Article Title: Direct disassembly of α-syn preformed fibrils into native α-syn monomers by an all-D-peptide

    Journal: bioRxiv

    doi: 10.1101/2023.12.11.571053

    PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.
    Figure Legend Snippet: PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.

    Techniques Used: Incubation, Injection, Centrifugation, Gentle

    (A) De novo ThT assay of 10 µM α-syn with and without 20 µM SVD-1a. ThT fluorescence progression was measured in a 96-well non-binding half-area plate (Corning, USA) with a Fluorostar platereader (BMG labtech, GE) at λex = 448 nm and λem = 482 nm with 300 rpm continuous orbital shaking between reads. Data are shown as mean values with ± SD (n = 5). ( B ) CD secondary structure analysis of de novo aggregation samples. Samples were incubated as described in (A) without added ThT (n = 3) and subsequently pooled for CD analysis. Far-UV ellipticity of the samples was measured in a quartz cuvette (l = 10 mm) in a J-1100 CD-spectrometer (Jasco, GE). In addition to (A), a sample with 20 µM SVD-1a alone was incubated under identical conditions and later used as reference for the sample with α-syn and SVD-1a. For this sample (α-syn + SVD-1a (after incubation)) the SVD-1a reference subtracted CD spectrum is shown. ( C ) Samples from (A) were isolated directly after incubation and diluted in PBS pH 7.4 to a final concentration of 1 µM α-syn monomer equivalent. 5 µl diluted sample was incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The section shown in (C) are representative for the observed species identified on all surface sections.
    Figure Legend Snippet: (A) De novo ThT assay of 10 µM α-syn with and without 20 µM SVD-1a. ThT fluorescence progression was measured in a 96-well non-binding half-area plate (Corning, USA) with a Fluorostar platereader (BMG labtech, GE) at λex = 448 nm and λem = 482 nm with 300 rpm continuous orbital shaking between reads. Data are shown as mean values with ± SD (n = 5). ( B ) CD secondary structure analysis of de novo aggregation samples. Samples were incubated as described in (A) without added ThT (n = 3) and subsequently pooled for CD analysis. Far-UV ellipticity of the samples was measured in a quartz cuvette (l = 10 mm) in a J-1100 CD-spectrometer (Jasco, GE). In addition to (A), a sample with 20 µM SVD-1a alone was incubated under identical conditions and later used as reference for the sample with α-syn and SVD-1a. For this sample (α-syn + SVD-1a (after incubation)) the SVD-1a reference subtracted CD spectrum is shown. ( C ) Samples from (A) were isolated directly after incubation and diluted in PBS pH 7.4 to a final concentration of 1 µM α-syn monomer equivalent. 5 µl diluted sample was incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The section shown in (C) are representative for the observed species identified on all surface sections.

    Techniques Used: ThT Assay, Fluorescence, Binding Assay, Incubation, Isolation, Concentration Assay, Gentle

    j 1100 cd spectrophotometer  (JASCO Inc)


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    JASCO Inc j 1100 cd spectrophotometer
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    JASCO Inc j 1100 spectrophotometer
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    j 1100 spectrophotometer  (JASCO Inc)


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    JASCO Inc j 1100 spectrophotometer
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    j 1100 spectropolarimeter  (JASCO Inc)


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    JASCO Inc j 1100 spectropolarimeter
    J 1100 Spectropolarimeter, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    j 1100 spectrometer  (JASCO Inc)


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    JASCO Inc j 1100 spectrometer
    J 1100 Spectrometer, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    j 1100 cd spectrometer  (JASCO Inc)


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    JASCO Inc j 1100 cd spectrometer
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    JASCO Inc j 1100 spectropolarimeter
    PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system <t>(J-1100,</t> JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.
    J 1100 Spectropolarimeter, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    JASCO Inc j 1100 spectrophotometer
    PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system <t>(J-1100,</t> JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.
    J 1100 Spectrophotometer, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    JASCO Inc j 1100 spectrometer
    PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system <t>(J-1100,</t> JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.
    J 1100 Spectrometer, supplied by JASCO Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    JASCO Inc j 1100 cd spectrometer
    PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system <t>(J-1100,</t> JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.
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    PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.

    Journal: bioRxiv

    Article Title: Direct disassembly of α-syn preformed fibrils into native α-syn monomers by an all-D-peptide

    doi: 10.1101/2023.12.11.571053

    Figure Lengend Snippet: PFF oligomers were prepared as described previously. 100 nM monomer equivalent PFF oligomers were incubated with or without 400 nM and 1600 nM SVD-1a for 3 d at 37 °C in PBS pH 7.4. ( A ) HPLC-SEC measurement samples were injected on a Bio SEC-3 column (300 Å, Agilent, USA). The PFF oligomers elute after approx. 5 min, while α-syn monomer is detected after approx. 8.6 min. ( B ) Time dependent DLS measurements with 100 nM PFF oligomers in presence (red) and absence (black) of 400 nM SVD-1a. 1 ml sample was continuously measured in a sealed quartz cuvette at 37 °C under quiescent condition every 30 s for 72 h in a SpectroSize 300 instrument (XtalConcepts, GE). Data are shown as radius plot where the signal amplitude of each particle size is represented by the data point diameter. ( C ) For AFM analysis 5 µl of the samples as described in (A) was rescued before centrifugation and incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The sections shown in C are representative for the observed species and particle density identified on all surface sections.

    Article Snippet: Far-UV circular dichroism (CD) data were collected using a Jasco J-1100 spectropolarimeter (Jasco, GE).

    Techniques: Incubation, Injection, Centrifugation, Gentle

    (A) De novo ThT assay of 10 µM α-syn with and without 20 µM SVD-1a. ThT fluorescence progression was measured in a 96-well non-binding half-area plate (Corning, USA) with a Fluorostar platereader (BMG labtech, GE) at λex = 448 nm and λem = 482 nm with 300 rpm continuous orbital shaking between reads. Data are shown as mean values with ± SD (n = 5). ( B ) CD secondary structure analysis of de novo aggregation samples. Samples were incubated as described in (A) without added ThT (n = 3) and subsequently pooled for CD analysis. Far-UV ellipticity of the samples was measured in a quartz cuvette (l = 10 mm) in a J-1100 CD-spectrometer (Jasco, GE). In addition to (A), a sample with 20 µM SVD-1a alone was incubated under identical conditions and later used as reference for the sample with α-syn and SVD-1a. For this sample (α-syn + SVD-1a (after incubation)) the SVD-1a reference subtracted CD spectrum is shown. ( C ) Samples from (A) were isolated directly after incubation and diluted in PBS pH 7.4 to a final concentration of 1 µM α-syn monomer equivalent. 5 µl diluted sample was incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The section shown in (C) are representative for the observed species identified on all surface sections.

    Journal: bioRxiv

    Article Title: Direct disassembly of α-syn preformed fibrils into native α-syn monomers by an all-D-peptide

    doi: 10.1101/2023.12.11.571053

    Figure Lengend Snippet: (A) De novo ThT assay of 10 µM α-syn with and without 20 µM SVD-1a. ThT fluorescence progression was measured in a 96-well non-binding half-area plate (Corning, USA) with a Fluorostar platereader (BMG labtech, GE) at λex = 448 nm and λem = 482 nm with 300 rpm continuous orbital shaking between reads. Data are shown as mean values with ± SD (n = 5). ( B ) CD secondary structure analysis of de novo aggregation samples. Samples were incubated as described in (A) without added ThT (n = 3) and subsequently pooled for CD analysis. Far-UV ellipticity of the samples was measured in a quartz cuvette (l = 10 mm) in a J-1100 CD-spectrometer (Jasco, GE). In addition to (A), a sample with 20 µM SVD-1a alone was incubated under identical conditions and later used as reference for the sample with α-syn and SVD-1a. For this sample (α-syn + SVD-1a (after incubation)) the SVD-1a reference subtracted CD spectrum is shown. ( C ) Samples from (A) were isolated directly after incubation and diluted in PBS pH 7.4 to a final concentration of 1 µM α-syn monomer equivalent. 5 µl diluted sample was incubated and dried on a freshly cleaved mica surface followed by washing with ddH 2 O and drying using a gentle stream of N 2 . Analysis was performed using NanoWizard 3 system (J-1100, JPK BioAFM, USA), recording multiple surface sections. The section shown in (C) are representative for the observed species identified on all surface sections.

    Article Snippet: Far-UV circular dichroism (CD) data were collected using a Jasco J-1100 spectropolarimeter (Jasco, GE).

    Techniques: ThT Assay, Fluorescence, Binding Assay, Incubation, Isolation, Concentration Assay, Gentle