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Lamda 25 spectrophotometer

Manufactured by PerkinElmer
Sourced in Germany, United States

The Lamda 25 spectrophotometer is a laboratory instrument used to measure the absorption or transmission of light by a sample across a specified wavelength range. It is designed to quantify the concentration of a particular substance in a solution by analyzing the interaction between the sample and incident light.

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5 protocols using lamda 25 spectrophotometer

1

Characterization of Nanostructured Materials

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The SEM images and EDS analysis were acquired using a Hitachi SU-8010 equipped with an EDX analyzer operated at an accelerating voltage of 5 kV. The TEM images were obtained on a JEM 2100 operating at 200 kV. The UV-vis diffuse reflectance spectroscopy (DRS) measurements were obtained on a UV-vis spectrometer (Shimadzu UV-2550) using BaSO4 as a reference standard. The specific surface area of the samples was measured by the Brunauer–Emmett–Teller (BET) method using nitrogen adsorption and desorption isotherms on a Micrometrics ASAP 2020 system. The UV-vis spectra were obtained on a Perkin Elmer Lamda 25 spectrophotometer. The NMR spectra were recorded on a Mercury Vx-300 MHz NMR spectrometer. XRD patterns were obtained on a Bruker D8-Advance. The luminescence spectra were measured using a Hitachi F-4500 spectrophotometer in MeOH at room temperature. A 500 W xenon lamp (CHFXQ 500 W, Global xenon lamp power) with a λ ≥ 420 nm optical filter, AM 1.5 optical filter and a heat cut-off filter provided visible light or simulated sunlight illumination.
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2

Liposomal Rhodamine Encapsulation Efficiency

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The EE% data was obtained by UV-VISIBLE spectra, recorded at 25 °C with a Perkin-Elmer Lamda 25 spectrophotometer (10 mm cuvettes). Before spectra recording, liposome disruption was carried out to dispose of the scattering background (scaling as λ-4), due to large aggregates in solution, which can affect precise intensity evaluation. To disrupt liposomes and release the entrapped rhodamine, samples underwent several cycles of freezing (−32 °C). A calibration curve was built by measuring the absorbance of solutions with known rhodamine concentration at 530 nm.
Encapsulation efficiency (EE%) describes the amount of drug encapsulated in the liposome relative to the total amount of drug used in liposomal synthesis. The EE% can be calculated using the following equation:
where Tdrug is the total amount of drug added during synthesis and Edrug is the experimentally determined amount of drug.
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3

Oligonucleotide-Based Biomolecular Assay

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Unmodified oligonucleotides were purchased from Biomers (Ulm, Germany) or IDT‐DNA (Leuven, Belgium) in HPLC‐purified form and were used without modification. Strand IX‐1 was prepared as described in the Supporting Information, using a known C3 linker phosphoramidite.19 Flavin adenine dinucleotide (FAD) was from Alfa Aesar (Karlsruhe, Germany); ATP and protamine from Salmon (grade IV, histone‐free) were from Sigma–Aldrich (Taufkirchen, Germany). The flow apparatus contained a MasterFlex C L−1 peristaltic pump, model No. 77122‐14, (Cole Palmer, Vernon Hills, Illinois), a QS 10 flow cuvette (Hellma Analytics, Müllheim, Germany), a Lamda 25 spectrophotometer (PerkinElmer, Rodgau, Germany) with Peltier‐controlled six‐cell holder, and silicon tubing with 1 mm inner diameter (Carl Roth, Karlsruhe, Germany). The membranes (5 mm diameter) used in the flow cell were from synthesis columns for automated DNA‐synthesis from Sigma–Aldrich (Taufkirchen, Germany). The luciferase luminescence assay used an ATP Biomass Kit HS (BioThema, Handen, Sweden).
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4

Comprehensive Characterization of Amino Acid-Capped ZnS:Mn Nanoparticles

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The UV/visible spectra in Figure 1a were obtained using a Lamda-25 spectrophotometer (Perkin-Elmer, Waltham, MA, USA), and the room-temperature solution photoluminescence (PL) spectra in Figure 1b were obtained using an LS-45 spectrophotometer (Perkin-Elmer) equipped with a 500 W xenon lamp as a light source. The presented pictures of high-resolution-transmission electron microscopy (HR-TEM in Figures 2 and 3) were obtained using a JEOL JEM 1210 electron microscope, in which the magnification range was from 1000 to 800,000, and the accelerating voltage was from 40 to 120 kV. The powder X-ray diffraction (XRD) pattern diagrams of the NPs presented in Figure 4 were obtained using an X-ray diffractometer, Rigaku 300, which used a Cu-Kα (wavelengths of 1.54 Å) X-ray light source. The elemental analyses for the Gly-ZnS:Mn, Ala-ZnS:Mn, and Val-ZnS:Mn nanoparticles were performed using a Perkin-Elmer Optima-430 ICP-AES spectrometer. The surface capping ligands, i.e., amino acids (Gly, Ala, and Val), were investigated in terms of their specific vibrational modes using Fourier-transform infrared spectroscopy (FT-IR, in Figure 5) recorded using a Spectrum One spectrophotometer (Perkin-Elmer, resolution of 1.0 cm−1) having an attenuated total reflection (ATR) unit. The number of scans was set to 32 for the liquid samples of the NPs.
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5

UV Melting of Oligonucleotides with Ligands

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The UV melting curves were measured on a Lamda 25 spectrophotometer (Perkin Elmer) with peltier-based temperature control. Sample were 1 µM oligonucleotides in 10 mM phosphate buffer, 1 M NaCl, pH = 6.0 with or without 5 µM ligand. Absorption was measured at 260 nm in the temperature range between 5 °C and 85 °C with a heating and cooling rate of 1 °C min -1 . For each sample, two heating and cooling curves were recorded. The melting points were calculated as the extrema of the first derivation of the heating curves using UV-WinLab (Perkin Elmer).
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