A freshly prepared stock solution of CR (7.0 mg/mL) in 10 mM phosphate buffer at pH 7.4 was filtered through 0.22 μm syringe and then diluted in water at 5.0 μM final concentration. This solution was incubated for 30 minutes at room temperature with 0.5 mg/mL of Aβ16‐21 peptide. After incubation, UV‐Vis spectra of Congo Red (CR) alone or incubated with Aβ16‐21 were recorded between 400 and 750 nm on Nanodrop 2000c spectrophotometer equipped with a 1.0 cm quartz cuvette (Hellma).
1.0 cm quartz cuvette
Manufactured by Hellma
Sourced in United States
The 1.0 cm quartz cuvette is a laboratory equipment used for spectroscopic analysis. It is made of quartz and has a path length of 1.0 centimeters, providing a consistent optical path for sample measurements.
Automatically generated - may contain errors
Lab products found in correlation
Nanodrop 2000c spectrophotometer, by Hellma (7 mentions)
Nanodrop 2000c, by Hellma (3 mentions)
Uv vis, by Thermo Fisher Scientific (3 mentions)
Lyophilized fmoc ff powder, by Bachem (2 mentions)
Span 60, by Merck Group (2 mentions)
Tween 60, by Merck Group (2 mentions)
Citrate acid, by Merck Group (1 mentions)
Lc8 hplc system, by Shimadzu (1 mentions)
Sodium chloride (nacl), by Merck Group (1 mentions)
Sodium citrate, by Merck Group (1 mentions)
Nanodrop 2000c spectrophotometer, by Thermo Fisher Scientific (1 mentions)
11 protocols using 1.0 cm quartz cuvette
1
Spectrophotometric Analysis of Amyloid-β
2
Synthesis of Radiolabeled Peptide Conjugates
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Protected Nα-Fmoc-amino acid derivatives, coupling reagents, and Rink amide 4-methylbenzhydrylamine (MBHA) resin were purchased from Calbiochem-Novabiochem (Laufelfingen, Switzerland). The Fmoc-21-amino-4,7,10,13,16,19-hexaoxaheneicosanoic acid (Fmoc-Ahoh-OH) and Fmoc-8-amino-3,6-dioxaoctanoic acid (Fmoc-AdOO-OH) were purchased from Neosystem (Strasbourg, France). DOTA(OtBu)3-OH (1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetate tert-butyl ester) was purchased from CheMatech (Dijon, France). Citrate acid, sodium citrate, and sodium chloride were obtained from Sigma-Aldrich Corp. (St. Louis, MO, USA). All other chemicals were commercially available by Sigma-Aldrich, Fluka (Bucks, Switzerland) or LabScan (Stillorgan, Dublin, Ireland) and were used as received unless otherwise stated. Preparative HPLCs were carried out on a LC8 Shimadzu HPLC system (Shimadzu Corporation, Kyoto, Japan) equipped with a UV Lambda-Max Model 481 detector. UV-Vis measurements were carried out on Thermo Fisher Scientific Inc. (Wilmington, Delaware USA) Nanodrop 2000c spectrophotometer equipped with a 1.0-cm quartz cuvette (Hellma). 177LuCl3 and 111InCl3 were obtained from IDB (Petten, The Netherlands) and Mallinckrodt Radiopharmaceuticals Italia (Segrate, Italy), respectively.
3
Fmoc-FF Peptide Characterization Protocol
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Lyophilized Fmoc-FF powder was purchased from Bachem (Bubendorf, Switzerland). TWEEN® 60, SPAN® 60, oil mineral, and all other chemicals were purchased from Sigma-Aldrich, Fluka (Bucks, Switzerland) or LabScan (Stillorgan, Dublin, Ireland) and were used as received unless otherwise stated. All solutions were obtained by weight using doubly distilled water as a solvent. The effective peptide concentrations in solution were spectroscopically determined by UV-Vis measurements on a nanodrop 2000c spectrophotometer (Thermo Fisher Scientific Inc., Wilmington, DE, USA) equipped with a 1.0 cm quartz cuvette (Hellma) using as molar absorptivity (ε) the values of 7800 mol−1 L cm−1 at 301 nm.
4
Peptide Solutions Preparation and Characterization
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2Nal2 and Gd-2Nal2 peptide solutions were prepared by dissolving the lyophilized powder in double distilled water. The concentration of the final solution was determined by absorbance on UV-vis Thermo Fisher Scientific Inc (Wilmington, Delaware USA) Nanodrop 2000c spectrophotometer using a 1.0 cm quartz cuvette (Hellma). The molar absorptivity (ε280) for 2Nal2 and Gd-2Nal2 peptide employed for the spectroscopic measurements was 6070 M−1 cm−1.
5
Peptide Concentration Determination
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PEG6-Y4 solutions were prepared dissolving the pure peptide powder in water at the desired concentration. The effective peptide concentration in solution was spectroscopically determined by UV–Vis measurements on Thermo Fisher Scientific Inc (Wilmington, Delaware USA) Nanodrop 2000c spectrophotometer equipped with a 1.0 cm quartz cuvette (Hellma) using as molar absorptivity (ε) the value of 5360 M−1·cm−142 (link).
6
Peptide Hydrogel Formation and Characterization
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Peptide
solutions were prepared by direct dissolution of pure powders in bidistilled
water. The analytical concentration of solutions was spectroscopically
determined by absorbance on a UV–vis Thermo Fisher Scientific
Inc. (Wilmington, Delaware, USA) Nanodrop 2000c spectrophotometer
equipped with a 1.0 cm quartz cuvette (Hellma) using the molar absorptivity
(ε) at 280 nm reported inTable 1 . For each peptide, the ε was calculated using
the formula ε(280)= [x·5500
+ y·1215 + k·2630] [L·cm–1·mol–1], where x, y, and k were the numbers of
W, Y, and Dopa residues, respectively. The solubility values analytically
determined were 1.15, 3.77, 7.61, and 15.00 mg/mL for (WY)3, PEG8-(WY)3,
(W-Dopa)3, and PEG8-(W-Dopa)3, respectively. Hydrogel formation was
triggered using the “solvent switch” method, which consists
of the addition of water to a peptide stock solution (100 mg/mL in
DMSO). The peptide concentration after water addition was 1.0 wt %
(10.0 mg/mL).
solutions were prepared by direct dissolution of pure powders in bidistilled
water. The analytical concentration of solutions was spectroscopically
determined by absorbance on a UV–vis Thermo Fisher Scientific
Inc. (Wilmington, Delaware, USA) Nanodrop 2000c spectrophotometer
equipped with a 1.0 cm quartz cuvette (Hellma) using the molar absorptivity
(ε) at 280 nm reported in
the formula ε(280)= [x·5500
+ y·1215 + k·2630] [L·cm–1·mol–1], where x, y, and k were the numbers of
W, Y, and Dopa residues, respectively. The solubility values analytically
determined were 1.15, 3.77, 7.61, and 15.00 mg/mL for (WY)3, PEG8-(WY)3,
(W-Dopa)3, and PEG8-(W-Dopa)3, respectively. Hydrogel formation was
triggered using the “solvent switch” method, which consists
of the addition of water to a peptide stock solution (100 mg/mL in
DMSO). The peptide concentration after water addition was 1.0 wt %
(10.0 mg/mL).
7
Peptide Characterization and Preparation
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PEG24‐F6 solution was prepared by dissolving the lyophilized powder in double distilled water sonicating the sample for 1 minutes. Then peptide concentration was determined with UV‐Vis Thermo Fisher Scientific Inc (Wilmington, Delaware USA) Nanodrop 2000c spectrophotometer equipped with a 1.0 cm quartz cuvette (Hellma) using a molar absorptivity (ϵ257) of 1170 M−1 cm−1. The peptide solution was diluted at 10 mg/mL. Solutions of H+‐Aβ16‐21‐O− at 5.0 and 100 mg/mL were prepared in water or in HFIP, respectively. The peptide concentration in water was assessed by UV‐Vis spectroscopy using of 390 M−1⋅cm−1 as molar absorptivity at 257 nm. Finally, stock solution of H+‐F6‐O− was prepared dissolving the peptide powder directly in 1,1,1,3,3,3‐hexafluoro‐2‐propanol (HFIP) at 50 mg/mL. Subsequently, this solution was also diluted with HFIP to obtain a concentration of 5.0 mg/mL. For solid state characterization, these peptide solutions were drop‐casted onto flat microscope glass slides and allowed to air dry at room temperature.
8
Quantification of Peptide Concentrations
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Peptide solutions were prepared by dissolving 10 mg of each lyophilized peptide in 1.0 mL of water. These suspensions were sonicated for 30 min at room temperature; after centrifugation (5 min at 13,000 rpm), the concentration was spectroscopically determined on UV–Vis Thermo Fisher Scientific Inc. (Wilmington, DE, USA) NanoDrop 2000 c spectrophotometer equipped with a 1.0 cm quartz cuvette (Hellma). The quantification of the concentration was assessed using the molar absorptivity (ε) of 7800 M−1 cm−1 for Fmoc group at λ = 301 nm.
9
Preparation and Characterization of Amyloid-beta Peptide Solutions
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Ac-F6-O−, H+-F6-Am and Ac-F6-Am solutions were prepared dissolving peptide powders directly in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) at 100 mg/mL. For H+-F6-O−, solution concentration was 50 mg/mL. Subsequently, these solutions were properly diluted with HFIP at the final required concentration. Ac-Aβ16–21-Am peptide solution was prepared directly dissolving lyophilized powder in double distilled water. The experimental concentration was assessed by UV–Vis spectroscopy carried out on UV–Vis Thermo Fisher Scientific Inc (Wilmington, Delaware USA) Nanodrop 2000c spectrophotometer using a 1.0 cm quartz cuvette (Hellma) and a molar absorptivity (ε257) of 390 M−1/cm. Then, these peptide solutions were drop-casted onto flat microscope glass slides and allowed to air dry at room temperature.
10
Synthesis and Characterization of Pegylated Liposomal Doxorubicin
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Protected Nα-Fmoc-amino acid derivatives, coupling reagents, and Rink amide MBHA (4-methylbenzhydrylamine) resin were purchased from Calbiochem-Novabiochem (Laufelfingen, Switzerland). The monodisperse Fmoc-8-amino-3,6-dioxaoctanoic acid (Fmoc- AdOO-OH, PEG2) was purchased from Neosystem (Strasbourg, France). Lyophilized Fmoc-FF powder was purchased from Bachem (Bubendorf, Switzerland). Doxorubicin chlorohydrate (Dox.HCl) was purchased from Sigma Aldrich (Milan, Italy). Pegylated liposomal Dox (commercial name of Doxil) vials were kindly gifted by the Italian Cancer Institute in Naples (Italy) “Fondazione G. Pascale”. TWEEN®60, SPAN®60, and all other chemicals and solvents were purchased from Sigma-Aldrich, Fluka (Bucks, Switzerland) or LabScan (Stillorgan, Dublin, Ireland) and were used as received unless otherwise stated. All solutions were obtained by weight using doubly distilled water as a solvent. UV-Vis spectra were recorded on a Thermo Fisher Scientific Inc (Wilmington, Delaware USA) Nanodrop 2000c, equipped with a 1.0 cm quartz cuvette (Hellma).
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