Ft ir 6100 fourier transform ir spectrometer

The melting points were obtained in open capillary tubes using an Electrothermal IA9100 digital melting point apparatus. Elemental microanalyses were carried out at the Micro Analytical Unit at Cairo University. ¹H NMR and ¹³C NMR spectra were recorded on a Bruker High Performance Digital FT-NMR Spectrometer Advance III (400/100 MHz) in the presence of TMS as the internal standard at Ain Shams University, Cairo, Egypt. Infrared spectra were measured using the KBr disc technique on a Jasco FT/IR-6100 Fourier transform IR spectrometer (Japan) at the scale of 400–4000 cm⁻¹. ESI-mass spectra were determined using an Advion Compact Mass Spectrometer (CMS), NY, USA. TLC on silica gel-precoated aluminum sheets (Type 60, F 254, Merck, Darmstadt, Germany) was used for following up the reactions and checking the purity of the chemical compounds using chloroform/methanol (3:1, v/v), and spots were detected with iodine vapor or through exposure to a UV lamp at δ 254 nm for several seconds. The nomenclature of the compounds is according to the IUPAC system. The starting compounds, 3-amino-thieno[2,3-b]pyridine-2-carboxamides (1a,b), were prepared using the reported method [56 (link)].

In situ FT-IR measurements were performed using an IRT-7000 IR microscope combined with an FT/IR-6100 Fourier transform IR spectrometer (Jasco Co., Tokyo, Japan). The IR absorption spectra were acquired in reflection mode using a 16× Cassegrain lens and 30-μm × 30-μm apertures and collected in the mid-IR range of 700–4000 cm^-1 at a resolution of 4 cm^-1 over 64 scans. Reflection spectra were obtained from areas around blood vessels in the cerebral cortex using the lattice measurement method (x-axis: 7 points, y-axis: 7 points, total of 49 spectra acquired). Each spectrum was deconvoluted for protein secondary structural analysis. The averaged contents of the main protein conformations (α-helix, β-sheet, β-turn, and random coil) were estimated by measuring peak intensities around the amide I bands (1600–1700 cm^-1), and were visualized using the universal RGB code on the protein mapping analysis software (IR-SSE; JASCO Co., Ltd) (Sarver and Krueger, 1991 (link)). Smoothing and normalization of spectra were performed on the region containing the amide bands (1000–2000 cm^-1) using Spectra Manager software Ver. 2 (Jasco International Co., Ltd, Tokyo, Japan).