Optical batch rebinding experiments were recorded with a Shimadzu UV-1900i spectrophotometer. To establish the binding affinity of the MIP/NIP, 20 mg of MIP/NIP particles were incubated with 5 mL solutions of melamine in Milli-Q water, with a concentration range from 0.02 to 0.5 mM. The samples were then shaken at 130 rpm for 90 min. The suspensions were then left to settle, after which the filtrate was collected and analyzed using a UV–VIS spectrophotometer. The remaining unbound concentration of melamine (Cf) in solution was then determined by UV–VIS spectroscopy, using a calibration curve for melamine that was generated prior at λ max (235 nm) (Figure S1 ).
Uv 1900i spectrophotometer
Manufactured by Shimadzu
Sourced in Japan
The UV-1900i spectrophotometer is a laboratory instrument manufactured by Shimadzu. It is designed to measure the absorbance or transmittance of light by a sample over a range of ultraviolet and visible wavelengths.
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Lab products found in correlation
Ht7700 microscope, by Hitachi (2 mentions)
1 ethyl 3 3 dimethylaminopropyl carbodiimide hydrochloride, by Thermo Fisher Scientific (1 mentions)
Rf 6000 spectrofluorophotometer, by Shimadzu (1 mentions)
N hydroxysulfosuccinimide sodium salt nhs, by Thermo Fisher Scientific (1 mentions)
Dulbecco s phosphate buffered saline, by Thermo Fisher Scientific (1 mentions)
Nano zs90, by Agilent Technologies (1 mentions)
Nicolet is5 infrared spectrometer, by Thermo Fisher Scientific (1 mentions)
Starch, by Merck Group (1 mentions)
18 protocols using uv 1900i spectrophotometer
1
Melamine binding affinity of MIP/NIP
2
Enzymatic Activities Determination Protocol
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Enzyme activities were determined spectrophotometrically on a Shimadzu UV-1900i spectrophotometer (Japan) in quartz cuvettes with an optical path length of 1 cm at 25 °C.
The activity of catechol 1,2-dioxygenase (Cat 1,2-DO) (EC 1.13.11.1) was determined according to Hayaishi [31 (link)] with some modifications.
The activity of catechol 2,3-dioxygenase (Cat 2,3-DO) (EC 1.13.11.2) was determined as described earlier [32 (link)].
The activity of catalase (EC 1.11.1.6) in the supernatants was determined as hydrogen peroxide decomposition [33 (link)]. Catalase activity was calculated according to H2O2 molar extinction coefficient ε = 43,600 M−1 cm−1. The enzyme amount catalyzing the decomposition of 1 μmol H2O2 was used as an activity unit.
Activity of glutathione reductase (EC 1.6.4.2) was determined according to Li [34 (link)]. The activity according to the decrease in optical density at 340 nm was monitored (ε = 6.220 × 103 M−l cm−1). Activity was expressed in μmol NADPH/(min per mg of protein).
Protein concentration was measured using the modified Bradford method [35 (link)].
The activity of catechol 1,2-dioxygenase (Cat 1,2-DO) (EC 1.13.11.1) was determined according to Hayaishi [31 (link)] with some modifications.
The activity of catechol 2,3-dioxygenase (Cat 2,3-DO) (EC 1.13.11.2) was determined as described earlier [32 (link)].
The activity of catalase (EC 1.11.1.6) in the supernatants was determined as hydrogen peroxide decomposition [33 (link)]. Catalase activity was calculated according to H2O2 molar extinction coefficient ε = 43,600 M−1 cm−1. The enzyme amount catalyzing the decomposition of 1 μmol H2O2 was used as an activity unit.
Activity of glutathione reductase (EC 1.6.4.2) was determined according to Li [34 (link)]. The activity according to the decrease in optical density at 340 nm was monitored (ε = 6.220 × 103 M−l cm−1). Activity was expressed in μmol NADPH/(min per mg of protein).
Protein concentration was measured using the modified Bradford method [35 (link)].
3
Lipid-Conjugated Nanoparticle Synthesis
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All chemicals, including 4-amino-2,2,6,6-tetramethylpiperidine-1-oxyl (TEMPO, CAS# 14691-88-4), were purchased from Millipore Sigma (St. Louis, MO, USA) and used as received unless otherwise mentioned. The perylene (PY) dye was prepared as previously described [37 (link)]. Dulbecco’s phosphate-buffered saline (DPBS), 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES, 1M), Dulbecco’s Modified Eagle Medium (DMEM) containing 25 mM HEPES (DMEM-HEPES), live cell imaging solution (LCIS), 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC·HCl, CAS# 25952-53-8), N-hydroxysulfosuccinimide sodium salt (NHS, CAS# 106627-54-7), and the plasma membrane probe wheat germ agglutinin-Alexa Fluor™ 488 conjugate (WGA-AF488) were purchased from Thermofisher Scientific (Waltham, MA, USA). Poly (ethylene glycol) amine hydrochloride (PEG-NH2.HCl, MW 2000) was purchased from Nanocs Inc. (New York, NY, USA). Human 4-HNE competitive ELISA 96-well assay kit was purchased from LifeSpan Biosciences, Inc. (Seattle, WA, USA). UV-Vis absorbance and fluorescence spectra of the LCNPs were measured on a UV-1900i Spectrophotometer (Shimadzu Scientific Instruments, Columbia, MD, USA) and an RF-6000 Spectrofluorophotometer (Shimadzu Scientific Instruments, Columbia, MD, USA), respectively.
4
Spectroscopic Analysis of Silica and TEOS
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The absorption spectra of the SSilica and TEOS solutions, whose Si4+ ion concentrations were adjusted to 0.5 mmol g−1 by dilution with ethanol, were measured in the wavelength region of 200–600 nm using a UV-1900i spectrophotometer (Shimadzu, Kyoto, Japan) in the double-beam mode. Ethanol was used as a reference. The transmittance spectra of FCOMP and FCNT were measured in the range of 200–1100 nm in double-beam mode. A quartz glass substrate was used as a reference for the measurements.
5
Quantification of Total Phenolic Compounds
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The amount of total phenolic compounds was determined using the method of Singleton and Rossi (1965) and Singleton et al. (1999) with some modifications. 200 μL of sample were mixed with 1000 μL of Folin-Ciocalteu reagent (0.4 M aqueous solution) and allow to stand for 3 min. Then 1000 μL of Na2CO3 solution (5% w/v) was added and kept in the dark for 30 min. The absorbance of the samples was read at 765 nm using a Shimadzu UV-1900i spectrophotometer (Tokyo, Japan). To calculate the concentration, a standard curve (R2 = 0.987) was made with different concentrations of gallic acid (0–50 ppm). The content of total phenolic compounds was calculated as mg gallic acid equivalents (GAE) per gram of sample (mg GAE/g) in dry basis (db) and was calculated using Eq. (4) . where Abs is the absorbance of the sample, b the intercept (0.0064), m the slope (0.0008 1/ppm), and DF is the dilution factor.
6
Antioxidant Capacity Assessment of Powders
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The antioxidant capacity (AC) of all powders was determined by the inhibition of the DPPH● radical (2,2-diphenyl-1-picrylhydrazyl) (Sigma-Aldrich, MO, USA) method. 100 μL of each solution of powder was mixed with 2000 μL of DPPH ethanolic (0.04 M) solution. The DDPH-solution mixtures were kept in the dark for 30 min at room temperature. Subsequently, the absorbance at 517 nm was read in a Shimadzu UV-1900i spectrophotometer (Tokyo, Japan). The absorbance values were used to calculate the percentage of inhibition (I%) with Eq. (7) . where AbsDPPH is the absorbance value of 2,000 μL of DPPH with 100 μL of water, AbsSample is the absorbance of the DPPH-sample mixture after 30 min. The results of the antioxidant capacity were calculated as mg of Trolox equivalents (TE) per gram of sample (mg TE/g) in dry basis (db) and were calculated with Eq. (8) . where b is the intercept (1.107), m the slope (0.780 1/ppm) of a standard curve (R2 = 0.990) with different concentrations of Trolox (0–100 ppm), and DF is the sample dilution factor.
7
Antioxidant Enzyme Activity Detection
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The activities of superoxide dismutase (SOD), catalase (CAT), ascorbate peroxidase (APX), peroxidase (POD), glutathione reductase (GR), and glutathione-S-transferases (GST) were detected based on previously described methods: SOD (Wang et al., 2020 (link)), CAT (Yang et al., 2020 (link)), APX (Wang et al., 2017 (link)), POD (Wang et al., 2016b (link)), GR (Yin et al., 2017 (link)), and GST (Li et al., 2018 (link)). All samples were analyzed using a Shimadzu UV-1900i spectrophotometer.
8
UV-Vis Analysis of G-AgNP Solution
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To analyse the G-AgNP solution and measure the amount and dispersion of nanoparticles, a Shimadzu UV-1900i spectrophotometer (Tokyo, Japan) was used to record UV–Vis spectra, scanning the absorption spectra in the 300–700 nm wavelength range.
9
Proteolytic Activity Measurement Protocol
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Measurement of proteolytic activity was carried out according to the method of Anson [19 (link)] with modifications. Briefly, the reaction mixture consisted of 0.5 mL of 1% hemoglobin in 50 mM citrate buffer (pH 3.0) and 0.02 mL of enzyme. The mixture was incubated for 10 min at 37 °C. The reaction was stopped with 0.5 mL of 10% trichloroacetic acid. The optical density was measured at 280 nm on a UV-1900i spectrophotometer (Shimadzu, Kyoto, Japan). The amount of enzyme required to release 1 µg tyrosine per minute was taken as the unit of activity.
10
Quantifying Monomeric Anthocyanins in Samples
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The content of total monomeric anthocyanins was assessed using the differential pH spectrophotometric method (Lee et al., 2005 ). Briefly, one mL of sample was mixed with 4 mL of two different buffers separately (0.025M potassium chloride, pH 1.0, and 0.4M acetate buffer, pH 4.5). Mixtures were allowed to stand for 15 min in the dark at room temperature. The absorbance of each sample was then read at the different pHs at 520 and 700 nm using a Shimadzu UV-1900i spectrophotometer (Tokyo, Japan). The absorbances were calculated using Eq. (5) .
The total monomeric anthocyanin content was calculated as the equivalents of peonidin-3,5-diglucoside (Pnd-3,5-diglu) per gram of sample (mg Pnd-3,5-diglu/g) in dry basis (db) usingEq. (6) . where Abs is the difference of absorbances, MW the molecular weight of Pnd-3,5-diglu (625.4 g/mol), DF is the dilution factor, V is the volume of the sample, 1000 is a conversion factor to mg, ε the molar absorptivity coefficient (36.654 L/cm mol) and l the pathway of light in the cell.
The total monomeric anthocyanin content was calculated as the equivalents of peonidin-3,5-diglucoside (Pnd-3,5-diglu) per gram of sample (mg Pnd-3,5-diglu/g) in dry basis (db) using
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