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multimode 8 model atomic force microscope (afm)  (Veeco)

 
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    Veeco multimode 8 model atomic force microscope (afm)
    Multimode 8 Model Atomic Force Microscope (Afm), supplied by Veeco, 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/result/multimode 8 model atomic force microscope (afm)/product/Veeco
    Average 90 stars, based on 1 article reviews
    multimode 8 model atomic force microscope (afm) - by Bioz Stars, 2026-03
    90/100 stars

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    Sequential protein adsorption on PGS substrates. ( a ) Atomic force <t>microscope</t> <t>(AFM)</t> height images of 2 × 2 µm 2 and ( b ) protein adsorption quantification from microBCA colorimetric technique with single protein (Fn 100 μg/mL or Col I 400 μg/mL) and sequential adsorption assays of Fn and Col I (Fn 100 μg/mL+ Col I 80 μg/mL), and vice versa (Col I 400 μg/mL + Fn 20 μg/mL) on PGS cured at different temperatures. The first column in ( a ) shows the presence of PGS on the glass with no major difference in height for any of the applied curing temperatures. All images share the 500 nm scale bar. Glass covers without spin-coated PGS are shown in ( b ) as control. Sample data distributions were analysed through two-way ANOVA and a Bonferroni post hoc multiple mean comparison test, with a p -value of 0.01.
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    Sequential protein adsorption on PGS substrates. ( a ) Atomic force <t>microscope</t> <t>(AFM)</t> height images of 2 × 2 µm 2 and ( b ) protein adsorption quantification from microBCA colorimetric technique with single protein (Fn 100 μg/mL or Col I 400 μg/mL) and sequential adsorption assays of Fn and Col I (Fn 100 μg/mL+ Col I 80 μg/mL), and vice versa (Col I 400 μg/mL + Fn 20 μg/mL) on PGS cured at different temperatures. The first column in ( a ) shows the presence of PGS on the glass with no major difference in height for any of the applied curing temperatures. All images share the 500 nm scale bar. Glass covers without spin-coated PGS are shown in ( b ) as control. Sample data distributions were analysed through two-way ANOVA and a Bonferroni post hoc multiple mean comparison test, with a p -value of 0.01.
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    Sequential protein adsorption on PGS substrates. ( a ) Atomic force <t>microscope</t> <t>(AFM)</t> height images of 2 × 2 µm 2 and ( b ) protein adsorption quantification from microBCA colorimetric technique with single protein (Fn 100 μg/mL or Col I 400 μg/mL) and sequential adsorption assays of Fn and Col I (Fn 100 μg/mL+ Col I 80 μg/mL), and vice versa (Col I 400 μg/mL + Fn 20 μg/mL) on PGS cured at different temperatures. The first column in ( a ) shows the presence of PGS on the glass with no major difference in height for any of the applied curing temperatures. All images share the 500 nm scale bar. Glass covers without spin-coated PGS are shown in ( b ) as control. Sample data distributions were analysed through two-way ANOVA and a Bonferroni post hoc multiple mean comparison test, with a p -value of 0.01.
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    90/100 stars
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    Bruker Corporation atomic force microscope afm model multimode 8 scanasyst
    Sequential protein adsorption on PGS substrates. ( a ) Atomic force <t>microscope</t> <t>(AFM)</t> height images of 2 × 2 µm 2 and ( b ) protein adsorption quantification from microBCA colorimetric technique with single protein (Fn 100 μg/mL or Col I 400 μg/mL) and sequential adsorption assays of Fn and Col I (Fn 100 μg/mL+ Col I 80 μg/mL), and vice versa (Col I 400 μg/mL + Fn 20 μg/mL) on PGS cured at different temperatures. The first column in ( a ) shows the presence of PGS on the glass with no major difference in height for any of the applied curing temperatures. All images share the 500 nm scale bar. Glass covers without spin-coated PGS are shown in ( b ) as control. Sample data distributions were analysed through two-way ANOVA and a Bonferroni post hoc multiple mean comparison test, with a p -value of 0.01.
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    Sequential protein adsorption on PGS substrates. ( a ) Atomic force microscope (AFM) height images of 2 × 2 µm 2 and ( b ) protein adsorption quantification from microBCA colorimetric technique with single protein (Fn 100 μg/mL or Col I 400 μg/mL) and sequential adsorption assays of Fn and Col I (Fn 100 μg/mL+ Col I 80 μg/mL), and vice versa (Col I 400 μg/mL + Fn 20 μg/mL) on PGS cured at different temperatures. The first column in ( a ) shows the presence of PGS on the glass with no major difference in height for any of the applied curing temperatures. All images share the 500 nm scale bar. Glass covers without spin-coated PGS are shown in ( b ) as control. Sample data distributions were analysed through two-way ANOVA and a Bonferroni post hoc multiple mean comparison test, with a p -value of 0.01.

    Journal: Polymers

    Article Title: Role of Curing Temperature of Poly(Glycerol Sebacate) Substrates on Protein-Cell Interaction and Early Cell Adhesion

    doi: 10.3390/polym13030382

    Figure Lengend Snippet: Sequential protein adsorption on PGS substrates. ( a ) Atomic force microscope (AFM) height images of 2 × 2 µm 2 and ( b ) protein adsorption quantification from microBCA colorimetric technique with single protein (Fn 100 μg/mL or Col I 400 μg/mL) and sequential adsorption assays of Fn and Col I (Fn 100 μg/mL+ Col I 80 μg/mL), and vice versa (Col I 400 μg/mL + Fn 20 μg/mL) on PGS cured at different temperatures. The first column in ( a ) shows the presence of PGS on the glass with no major difference in height for any of the applied curing temperatures. All images share the 500 nm scale bar. Glass covers without spin-coated PGS are shown in ( b ) as control. Sample data distributions were analysed through two-way ANOVA and a Bonferroni post hoc multiple mean comparison test, with a p -value of 0.01.

    Article Snippet: An atomic force microscope (AFM) (Bruker Multimode 8 model, Madrid, Spain) operating in tapping mode enabled the topography and composition of PGS substrates to be evaluated.

    Techniques: Adsorption, Microscopy, Control, Comparison