Journal:

Article Title: Intrinsic Determinants of Neurotoxic Aggregate Formation by the Amyloid β Peptide

doi: 10.1016/j.bpj.2009.12.4320

Figure Lengend Snippet: Measuring the neurotoxicity of Aβ mutants by their effect on fly longevity. (A) The average neurotoxicity (Stox) of a single line of flies expressing E22G Aβ42 (○) compared with that of two independent lines of flies expressing I31E/E22G Aβ42 (□ and ♢), one line of WT Aβ40 (Δ), and one line of WT Aβ42 (+). (B) The average neurotoxicity of a single line of flies expressing WT Aβ40 (○) or WT Aβ42 (♢) compared with those of two independent lines of flies expressing E3R Aβ40 (□ and Δ); 100 flies divided equally into 10 tubes were analyzed for each line. Stox for each tube (n = 10 flies per tube) was calculated from the median survival determined by Kaplan-Meier survival analysis (see Materials and Methods). Differences between lines (n = 10 tubes) were analyzed for significance using the Mann Whitney U-test (∗p < 0.05, ∗∗p < 0.01, and ∗∗∗p < 0.001).

Article Snippet: The A β peptides A β 40 , A β 42 , E22G A β 42, I31E/E22G A β 42 , and E3R A β 40 were purchased from Bachem (Weil am Rhein, Germany) dissolved in trifluoroacetic acid, and sonicated for 30 s on ice.

Techniques: Expressing, MANN-WHITNEY

Journal:

Article Title: Intrinsic Determinants of Neurotoxic Aggregate Formation by the Amyloid β Peptide

doi: 10.1016/j.bpj.2009.12.4320

Figure Lengend Snippet: Predicted aggregation propensity scores

Article Snippet: The A β peptides A β 40 , A β 42 , E22G A β 42, I31E/E22G A β 42 , and E3R A β 40 were purchased from Bachem (Weil am Rhein, Germany) dissolved in trifluoroacetic acid, and sonicated for 30 s on ice.

Techniques:

Journal:

Article Title: Intrinsic Determinants of Neurotoxic Aggregate Formation by the Amyloid β Peptide

doi: 10.1016/j.bpj.2009.12.4320

Figure Lengend Snippet: Aggregation propensity profiles of Aβ40 (solid line) and E22G Aβ42 (dashed line), indicating the locations in negative peaks of the two mutants studied here (E3R Aβ40 and I31E/E22G Aβ40).

Article Snippet: The A β peptides A β 40 , A β 42 , E22G A β 42, I31E/E22G A β 42 , and E3R A β 40 were purchased from Bachem (Weil am Rhein, Germany) dissolved in trifluoroacetic acid, and sonicated for 30 s on ice.

Techniques:

Journal:

Article Title: Intrinsic Determinants of Neurotoxic Aggregate Formation by the Amyloid β Peptide

doi: 10.1016/j.bpj.2009.12.4320

Figure Lengend Snippet: Measurement of the kinetics of aggregation and the types of aggregates formed by Aβ40, E22G Aβ42, and their mutants. (A) Progression of the aggregation reactions for E22G Aβ42 (solid circles) and E22G/I31E Aβ42 (open circles) monitored by ThT fluorescence spectroscopy. (B) The progression of the aggregation reactions for Aβ40 (solid squares) and E3R Aβ40 (open squares) was monitored by ThT fluorescence spectroscopy. (C and D) Transmission electron micrographs of samples from the end points of the E22G Aβ42 and I31E/E22G Aβ42 aggregation reactions shown in A indicate that fibrils were formed by both peptides. (E and F) Transmission electron micrographs of samples from the end points of the Aβ40 and E3R Aβ40 aggregation reactions shown in B indicate that fibrils were formed by both peptides. Scale bar = 200 μm.

Article Snippet: The A β peptides A β 40 , A β 42 , E22G A β 42, I31E/E22G A β 42 , and E3R A β 40 were purchased from Bachem (Weil am Rhein, Germany) dissolved in trifluoroacetic acid, and sonicated for 30 s on ice.

Techniques: Fluorescence, Spectroscopy, Transmission Assay

Journal:

Article Title: Intrinsic Determinants of Neurotoxic Aggregate Formation by the Amyloid β Peptide

doi: 10.1016/j.bpj.2009.12.4320

Figure Lengend Snippet: Time-course analysis by TEM of the aggregation of E22G Aβ42 and I31E/E22G Aβ42. (A–C) TEM images taken throughout the aggregation reaction of E22G Aβ42 (t = 0 min, 15 min, and 6 days, respectively). (D–F) TEM images taken throughout the aggregation reaction of I31E/E22G Aβ42 (0 min, 15 min, and 6 days, respectively). Scale bar = 200 nm. (G) The size distributions of aggregates of E22G Aβ42 (solid line) and E22G/I31E Aβ42 (dashed line) determined by SEC performed immediately after dissolution of the peptides.

Article Snippet: The A β peptides A β 40 , A β 42 , E22G A β 42, I31E/E22G A β 42 , and E3R A β 40 were purchased from Bachem (Weil am Rhein, Germany) dissolved in trifluoroacetic acid, and sonicated for 30 s on ice.

Techniques:

Journal: Chembiochem

Article Title: A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

doi: 10.1002/cbic.202400431

Figure Lengend Snippet: a) CD Spectra of 5 μM Aβ42 recorded at different time intervals in 10 mM phosphate buffer pH 7.4. b–d) CD difference spectra of Aβ42 in the presence of equimolar ration of conjugates: b) Cu‐Ph‐Pep ; c) Ph‐Pep ; d) Zn‐Ph‐Pep .

Article Snippet: Aβ42 peptide (20 μg/ml in Na Acetate pH 4.5) was immobilized on 4PCH WAVE chips (quasiplanar polycarboxylate surface; Creoptix) according to the manufacturer instructions at a final density of 1910±40 pg/mm 2 .

Techniques: Circular Dichroism

Journal: Chembiochem

Article Title: A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

doi: 10.1002/cbic.202400431

Figure Lengend Snippet: bis‐Ans Fluorescence intensities acquired for the a) binary systems Aβ42/ Cu‐Ph‐Pep ; Aβ42/ Ph‐Pep ; Aβ42/ Zn‐Ph‐Pep ; b) Cu‐Ph‐Pep ; Ph‐Pep ; Zn‐Ph‐Pep ; in the absence of Aβ42.

Article Snippet: Aβ42 peptide (20 μg/ml in Na Acetate pH 4.5) was immobilized on 4PCH WAVE chips (quasiplanar polycarboxylate surface; Creoptix) according to the manufacturer instructions at a final density of 1910±40 pg/mm 2 .

Techniques: Fluorescence

Journal: Chembiochem

Article Title: A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

doi: 10.1002/cbic.202400431

Figure Lengend Snippet: a) CD Spectra of Aβ42 (20 μM) in the Far‐UV region (195–350 nm) and near‐UV region (350–500 nm, inset). CD Spectra of Aβ42 in the presence of the porphyrin‐peptide conjugates (1 : 1 molar ratio) in the Far‐UV region (195–350 nm) and in the near‐UV region (350–500 nm, inset). b) Cu‐Ph‐Pep ; c) Ph‐Pep ; d) Zn‐Ph‐Pep . The signal at t=0 h was recorded in the interval 200–350 nm because below 200 nm the HT value was too high, and a distorted signal would be obtained (panel a).

Article Snippet: Aβ42 peptide (20 μg/ml in Na Acetate pH 4.5) was immobilized on 4PCH WAVE chips (quasiplanar polycarboxylate surface; Creoptix) according to the manufacturer instructions at a final density of 1910±40 pg/mm 2 .

Techniques: Circular Dichroism

Journal: Scientific Reports

Article Title: Amyloid β toxic conformer has dynamic localization in the human inferior parietal cortex in absence of amyloid plaques

doi: 10.1038/s41598-018-35004-3

Figure Lengend Snippet: Characterization of immunoreactivity of 11A1 antibody. ( A ) Assessment of the binding affinity of 11A1 antibody against various synthetic Aβ peptides. E22P-Aβ42 (green), E22P-Aβ9-35ox (black), E22P-Aβ11-35ox (red), E22P-Aβ16-35ox (blue), and E22P-Aβ11-34 (orange) were synthesized and the binding affinity of 11A1 antibody for each peptide was assessed by Enzyme immunoassay. The 11A1 antibody exhibited high binding affinity for E22P-Aβ42 and E22P-Aβ9-35ox. Data are expressed as mean ± SD of three independent measurements. ( B ) Comparison of 11A1 antibody staining pattern with that of 6E10, 4G8, and OC antibodies. Postmortem human frontal cortex sections of an Alzheimer’s disease patient were stained with 6E10 (left panel), 4G8 (center left panel), OC (center right panel) and 11A1 (right panel) antibodies. Senile plaques (arrow heads) and vascular amyloid (arrows) are identified by 11A1 antibody with a similar pattern to that of the other three Aβ antibodies. The images were taken under 20x objective lens. Scale bar 50 µm. ( C and D) Assessment of 11A1 cross-reactivity against APP. Histological sections of human cingulate gyrus with traumatic axonal injury were stained with 22C11 (APP antibody) (left panel) and 11A1 (right panel) antibodies. The traumatic axonal balloons display intense signal with the antibody for APP (arrowheads), but these lesions are not stained with 11A1 antibody. ( C ) The images were taken under 20x objective lens. Scale bar 50 µm. ( D ) The images were taken under 40x objective lens. Scale bar 20 µm. ( E ) Testing 11A1 antibody specificity for Aβ toxic conformer in senile plaques and blood vessels. 11A1 antibody was pre-incubated without (left panel) or with (right panel) its immunogen, E22P-Aβ9-35ox peptide, prior to incubation of tissues with the primary antibody. The pre-incubation with immunogen abrogates the signal in senile plaques and blood vessels. The images were taken under 20x objective lens. Scale bar 50 µm.

Article Snippet: The fragment peptides of E22P-Aβ42 for ElA of 11A1 were synthesized in a stepwise fashion on 0.1 mmol of preloaded Fmoc-L-Met-PEG-PS or Fmoc-L-Leu-PEG-PS resin by a synthesizer, Biotage ® initiator + Alstra TM (Biotage Japan) using the Fmoc method.

Techniques: Binding Assay, Synthesized, Enzyme-linked Immunosorbent Assay, Staining, Incubation

Journal: Scientific Reports

Article Title: Amyloid β toxic conformer has dynamic localization in the human inferior parietal cortex in absence of amyloid plaques

doi: 10.1038/s41598-018-35004-3

Figure Lengend Snippet: 11A1 immunoreactivity in pericapillary spaces. ( A and B ) Representative images were obtained under 63x objective lens. Pericapillary spaces in inferior parietal cortex, layer V, immunostained with 11A1 and Collagen IV. The rows of figures correspond to three age groups: early 30 s, middle 40 s, and early 60 s. Left panels show the 11A1 signal, middle panels indicate the Collagen IV signal and right panels show merged images. ( A ) Capillary cross sections, ( B ) capillary longitudinal sections. Scale bars ( A and B) , 5 µm. ( C ) Verification of 11A1 antibody’s specificity against Aβ toxic conformer in pericapillary space of the three age groups. The 11A1 antibody was pre-incubated with (bottom panels) or without (top panels) its immunogen, E22P-Aβ9-35ox peptide, prior to incubation of tissues with the primary antibody. The pre-incubation with immunogen abrogates the 11A1 signal around Collagen IV signal (magenta). Images were obtained under 20x objective lens. Scale bar 20 µm. ( D ) Percentage of pericapillary spaces labeled with 11A1 in measured area across age-spectrum (30-65 years). The relationship with age is not statistically significant before age 45 (p = 0.82), but it becomes highly significant after age 45 (p = 0.0006) by the Piecewise regression. ( E ) Number of cross sectional pericapillary spaces in measured area across age-spectrum (30–65 years). There is no significant change in the number of cross sectional capillary pericapillary spaces with age ( P = 0.496).

Article Snippet: The fragment peptides of E22P-Aβ42 for ElA of 11A1 were synthesized in a stepwise fashion on 0.1 mmol of preloaded Fmoc-L-Met-PEG-PS or Fmoc-L-Leu-PEG-PS resin by a synthesizer, Biotage ® initiator + Alstra TM (Biotage Japan) using the Fmoc method.

Techniques: Incubation, Labeling

Journal: Scientific Reports

Article Title: Amyloid β toxic conformer has dynamic localization in the human inferior parietal cortex in absence of amyloid plaques

doi: 10.1038/s41598-018-35004-3

Figure Lengend Snippet: 11A1 immunoreactivity in neurons. ( A and B ) Representative images were obtained under 63x objective lens. Cortical neurons of inferior parietal cortex, layer V, co-stained with 11A1 and MAP2 antibodies and 11A1, MAP2 and Cathepsin D antibodies. The rows of figures correspond to three age groups: early 30 s, middle 40 s, and early 60 s. ( A ) Left panels show the 11A1 signal (green), middle panels indicate MAP2 signal (red) and right panels show merged images. Scale bar 5 µm. ( B ) Left panels show the 11A1 signal, middle panels indicate Cathepsin D signal and right panels show merged images. The white contours in the merged images indicates the cell shape identified by MAP2. Intracellular 11A1 immunoreactivity (green) partially colocalized with Cathepsin D signal (Magenta). Scale bar 5 µm. ( C ) Verification of 11A1 antibody’s specificity against Aβ toxic conformer in neurons of the three age groups. 11A1 antibody was pre-incubated with (bottom panels) or without (top panels) its immunogen, E22P-Aβ9-35ox peptide, prior to incubation of tissue sections with the primary antibody. The pre-incubation with immunogen abrogates the 11A1 signal (green) in and around MAP2 signals (magenta). Images were obtained under 20x objective lens. Scale bar 20 µm. ( D ) Percentage of cortical neurons labeled with 11A1 in measured area across the age-spectrum (30–65 years). The relationship with age is not significant (p = 0.807). ( E ) Number of neurons in measured area across the age-spectrum (30–65 years). There is no significant change in the number of neurons with age (p = 0.6061).

Article Snippet: The fragment peptides of E22P-Aβ42 for ElA of 11A1 were synthesized in a stepwise fashion on 0.1 mmol of preloaded Fmoc-L-Met-PEG-PS or Fmoc-L-Leu-PEG-PS resin by a synthesizer, Biotage ® initiator + Alstra TM (Biotage Japan) using the Fmoc method.

Techniques: Staining, Incubation, Labeling

Journal: Scientific Reports

Article Title: Amyloid β toxic conformer has dynamic localization in the human inferior parietal cortex in absence of amyloid plaques

doi: 10.1038/s41598-018-35004-3

Figure Lengend Snippet: 11A1 immunoreactivity in protoplasmic astrocytes. ( A and B ) Representative images were obtained under 63x objective lens. Protoplasmic astrocytes of human inferior parietal cortex, layer V, immunostained with 11A1 and ALDH1L1 antibodies and 11A1, GFAP and Cathepsin D antibodies. The rows of figures correspond to three age groups: early 30 s, middle 40 s, and early 60 s. (A) Left panels show the 11A1 signal (green), middle panels correspond to the ALDH1L1 signal (red) and right panels show the merged images. Scale bar 5 µm. ( B ) Left panels show the 11A1 signal, middle panels correspond to the Cathepsin D signal (magenta) and right panels show the merged images. The white contours in the merged images indicate the cell shape identified by GFAP. Separate localization of the 11A1 immunoreactivity and Cathepsin D signals in the astrocytes is demonstrated. Scale bar 5 µm. ( C ) Verification of 11A1 antibody’s specificity against Aβ toxic conformer in protoplasmic astrocytes of the three age groups. The 11A1 antibody was pre-incubated with (bottom panels) or without (top panels) its immunogen, E22P-Aβ9-35ox peptide, prior to incubation of tissue sections with primary antibody. The pre-incubation with immunogen abrogates the 11A1 signal (green) in and around ALDH1L1 signal (magenta). Images were obtained under 20x objective lens. Scale bar 20 µm. ( D ) Percentage of protoplasmic astrocytes labeled with 11A1 of the astrocytes in measured area across the age-spectrum (30–65 years). The percentage of 11A1 labeled astrocytes gradually increases by age (p = 0.020). ( E ) Number of the astrocytes in measured area across the age-spectrum (30–65 years). Number of astrocytes gradually increases by age (p = 0.014).

Article Snippet: The fragment peptides of E22P-Aβ42 for ElA of 11A1 were synthesized in a stepwise fashion on 0.1 mmol of preloaded Fmoc-L-Met-PEG-PS or Fmoc-L-Leu-PEG-PS resin by a synthesizer, Biotage ® initiator + Alstra TM (Biotage Japan) using the Fmoc method.

Techniques: Incubation, Labeling

Journal: International Journal of Molecular Sciences

Article Title: Modified Low-Temperature Extraction Method for Isolation of Bletilla striata Polysaccharide as Antioxidant for the Prevention of Alzheimer’s Disease

doi: 10.3390/ijms222312760

Figure Lengend Snippet: The aggregation of Aβ42 into Aβ fibrils. ( a ) The fluorescence intensity of ThT was obtained by incubation of Aβ42 (Aβ; blue line), Aβ42 mixed with BSP (Aβ-BSP; red line) in PBS at 37 °C for 14 days. The green line represents the fluorescence intensity of ThT in PBS only (PBS). ( b ) The TEM image of Aβ42 monomers without aggregation on day 0; ( c ) the Aβ42 aggregated into thick and compact Aβ fibrils on day 7; ( d ) BSP reduced aggregation of Aβ42 with reduced thickness and loose packing of Aβ fibrils on day 7. The scale bar is 0.2 μm. ( n = 6, # p < 0.05 compared to control group, * p < 0.05 compared to Aβ group).

Article Snippet: Aβ42 peptides were synthesized by Gendanio Biotech Inc. (New Taipei City, Taiwan).

Techniques: Fluorescence, Incubation, Control

Journal: International Journal of Molecular Sciences

Article Title: Modified Low-Temperature Extraction Method for Isolation of Bletilla striata Polysaccharide as Antioxidant for the Prevention of Alzheimer’s Disease

doi: 10.3390/ijms222312760

Figure Lengend Snippet: The LIVE/DEAD staining of N2a cells in ( a ) the control: cells cultured in medium only, ( b ) positive control: cells treated with zinc diethyldithiocarbamate, ( c ) negative control: cells treated with aluminum oxide, ( d ) BSP: cells treated with an extracted solution of BSP, and ( e ) Aβ-BSP: cells treated with Aβ42 and BSP. ( f ) Quantitative results of survival rate in N2a cells. *** p < 0.001 compared with control.

Article Snippet: Aβ42 peptides were synthesized by Gendanio Biotech Inc. (New Taipei City, Taiwan).

Techniques: Staining, Control, Cell Culture, Positive Control, Negative Control

Journal: International Journal of Molecular Sciences

Article Title: Modified Low-Temperature Extraction Method for Isolation of Bletilla striata Polysaccharide as Antioxidant for the Prevention of Alzheimer’s Disease

doi: 10.3390/ijms222312760

Figure Lengend Snippet: Antioxidant activity of extracted BSP. DCFDA was used to measure the intracellular ROS in N2a cells without any treatment (control), treated with Aβ42 (Aβ), and Aβ42 and BSP (Aβ42-BSP). ( n = 6, # p < 0.05 compared to control group, * p < 0.05 compared to Aβ group).

Article Snippet: Aβ42 peptides were synthesized by Gendanio Biotech Inc. (New Taipei City, Taiwan).

Techniques: Antioxidant Activity Assay, Control

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Effect of bFg and hFg on the amyloid fibril formation of Aβ42. (A) Time courses of ThT fluorescence intensities with bFg (left) or hFg (right). Error bars represent one standard deviation ( n = 3). The lines indicate curves obtained by fitting using . (B) AFM image of an oligomer taken 1 h after incubation without bFg or hFg. Scale bar: 500 nm. (C) AFM image of amyloid fibrils taken 7 h after incubation without bFg or hFg. Scale bar: 500 nm. (D) The midpoint of the sigmoidal increase (τ half ) and the fluorescence intensity at the plateau phase ( I plat ) obtained from curve fitting of the data in panel A using . Error bars represent values obtained from curve fitting. The value for the control (without bFg or hFg) is indicated by black lines.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques: Fluorescence, Standard Deviation, Incubation, Control

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Dot blot results in the presence of bFg (A) or hFg (B), respectively. Samples were taken at 1 h after the start of amyloid fibril formation. Sample names are numbered and listed at the bottom of each panel. The intensities are normalized using that of Aβ42 only (sample ①). The error bars indicate one sigma values ( n = 3 ∼ 15). Examples of blots are shown below the bars.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques: Dot Blot

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: AUC profiles of Aβ42 in the presence of (A) bFg or (B) hFg at 1 h during amyloid fibril formation. Each panel displays an overview of the profiles (top) and magnified views along each axis (bottom). Each profile is shifted along the y -axis for clarity. Peaks marked with asterisks represent minor small components present in bFg or hFg.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques:

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Effect of bFg and hFg on Aβ42 oligomer formation, as observed in AFM images taken 1 h after the start of amyloid fibril formation. (A) Aβ42 only. (B) With 3 μM bFg. (C) With 3 μM hFg. Scale bars indicate 500 nm.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques:

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Cell viability in the presence of Aβ42 with or without bFg or hFg. Error bars represent ± 2 SD ( n = 3). P-values were obtained by a one-sided two-sample t test assuming equal variances.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques:

Journal: ACS Chemical Neuroscience

Article Title: Targeting Both Monomer and Oligomer with Fibrinogen Efficiently Suppresses Amyloid Fibril Formation and Cell Toxicity of Amyloid β 1‑42

doi: 10.1021/acschemneuro.5c00562

Figure Lengend Snippet: Proposed binding manners between Aβ42 and the fibrinogen molecules, and resultant effects on the inhibition of the Aβ42 amyloid fibril formation and cell toxicity. K d app values were obtained using eq S6 . The representations of the colors of bFg or hFg molecules are as follows: The N-terminal region of Aα chain, red; the C-terminal region of Aα chain, i.e., αC region, orange; the Bβ chain, blue; the γ chain, green. Globular domains are represented by ellipses. See details in the main text.

Article Snippet: Amyloid beta peptide (Aβ42) was purchased from Peptide Institute, Inc. (Japan) and used without further purification.

Techniques: Binding Assay, Inhibition