non-linear regression analysis with one site specific binding equation on graphpad prism Search Results


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(A) A <t>saturation</t> binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).
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(A) A <t>saturation</t> binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).
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(A) A <t>saturation</t> binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).
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(A) A <t>saturation</t> binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).
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(A) A <t>saturation</t> binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).
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(A) A <t>saturation</t> binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).
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(A) A saturation binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).

Journal: Bioconjugate chemistry

Article Title: Generation of clickable Pittsburgh Compound B for the detection and capture of β-amyloid in Alzheimer’s Disease brain

doi: 10.1021/acs.bioconjchem.7b00500

Figure Lengend Snippet: (A) A saturation binding assay was used to derive a Kd of 164.7 nM for fluorescent clicked PiB (4). (B) Dose-response curve showing displacement of fluorescent clicked PiB (4) (at 140 nM) with increasing concentrations (0–100,000 nM) of PiB (2) ( ) and clickable PiB (3) ( ). From these data, binding affinities (Ki) of 678.4 and 264.7 nM were determined for compounds 2 and 3, respectively (summarized in Table 1).

Article Snippet: Binding affinities were derived using the saturation binding one-site specific non-linear regression analysis model of GraphPad Prism 5 (GraphPad Software Inc., California).

Techniques: Saturation Assay, Binding Assay