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Schiff Bases

Schiff bases are a class of organic compounds formed by the condensation reaction between a primary amine and an aldehyde or ketone.
They play a crucial role in biological processes and have applications in various fields, including medicinal chemistry, catalysis, and materials science.
PubCompare.ai's AI-driven platform helps researchers explore this dynamic world of Schiff bases, providing access to the best protocols from literature, preprints, and patents.
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Most cited protocols related to «Schiff Bases»

1
Purification and Structural Analysis of Squid Rhodopsin
Cited 7 times
Purification of Squid Rhodopsin—All procedures were carried out at room temperature in the dark or under dim red light unless otherwise indicated. Squid rhodopsin was prepared from Todarodes pacificus caught in the Japan Sea, using previously described methods (13 ). Briefly, the rhabdomeric membranes were isolated from squid retina by repetitive sucrose flotation. The membranes were treated with V8 protease (Pierce, 50:1 w/w of rhodopsin:V8 protease) at room temperature for 1 h to remove the unique C-terminal proline-rich extension of the squid rhodopsin. The reaction was terminated by extensive washing with HEPES buffer (5 mm HEPES, pH 7.0, 1 mm EDTA, 1 mm dithiothreitol). The membranes were solubilized with 2% (w/v) dodecyl maltoside (DDM, Anatrace) for 1 h at 4 °C. After centrifugation, the supernatant was loaded onto a DEAE-cellulose column (Whatman) equilibrated with buffer A (50 mm HEPES, pH 7.0, 0.05% (w/v) DDM). The unbound fraction was collected and applied to a concanavalin A-Sepharose 4B column (Amersham Biosciences) equilibrated with buffer A. The rhodopsin was eluted with 0.2 m α-methyl mannoside solution. Fractions containing squid rhodopsin were pooled and dialyzed against buffer A and then concentrated by ultrafiltration (Amicon Ultra, Millipore).
N-terminal Sequencing and Mass Analyses—The identity and integrity of the purified protein were assessed by N-terminal amino acid sequencing by Edman degradation and various mass spectrometric analyses, including MALDI-TOF/MS, MALDI-TOF/TOF-MS/MS, nano-liquid chromatographyquadrapole TOF-MS/MS, and high performance liquid chromatography-electrospray ionization-iontrap-MS/MS as described in the supplemental materials (14 (link)).
Crystallization—Crystals were grown by the hanging-drop vapor diffusion method. One microliter of protein sample (10 mg/ml) in a solution of 10 mm HEPES, pH 7.0, 200 mm NaCl, 2 mm dodecyldimethylamine oxide, 0.03% (w/v) DDM was mixed with 1 μl of reservoir solution (0.1 m HEPES, pH 7.0, 8% (v/v) ethylene glycol, 28% (w/v) polyethylene glycol 400) and left to equilibrate at 20 °C. Crystals appeared after 5 days and stopped growing within 2 weeks.
Structure Determination and Refinement—X-ray diffraction data were collected at 100 K on beam line BL45XU at SPring-8. Data were reduced using the program HKL2000 (15 ). The structure was determined by molecular replacement with the program MOLREP in the CCP4 program suite (16 (link)) using a monomer of the trigonal crystal structure of the bovine rhodopsin (PDB code: 1GZM) (17 ) as a search model. Refinement and model building were performed iteratively with the programs CNS (18 (link)), REFMAC5 in CCP4 (16 (link)), and O (19 (link)). During refinement, we used grouped, unrestrained B-factor refinement with a single group for the entire molecule. All refinements were carried out with 10% of the reflections for cross validation. Despite the low resolution data and the low sequence homology between squid and bovine rhodopsins (24%), the structure was well refined thanks to the structural similarity of the transmembrane helices and the positions for a disulfide bridge, an 11-cis-retinal chromophore in the Schiff base linkage, and the conserved residues. B-factor sharpening was used to generate detailed maps using the CNS program with Bsharp values ranging from –50 to –150 Å2 (20 ). Data collection and refinement statistics are shown in Table 1. All figures including electrostatic potential surfaces were prepared using PyMOL (DeLano Scientific LLC). The coordinates have been deposited in the Protein Data Bank (PDB) with the accession code 2ZIY.

Data collection and refinement statistics

Data collection
    Wavelength (Å) 0.97950
    Resolution (Å) 43.2-3.7
    Measured reflections 43,571
    Unique reflections 6,680
    Completeness (%)a 93.3 (74.3)
    Rmerge (%)b 6.4 (77.5)c
    Space group C2221
    Unit cell (Å) a = 84.3, b = 108.7, c = 142.2
Refinement
    Resolution (Å) 43.2-3.7
    Reflections used 6,647
    Rwork/Rfree (%)d,e 30.2/33.0 (41.4/43.2)
    r.m.s.f deviation
        bond (Å) 0.014
        angle (°) 2.01
    Ramachandran statistics
        Most favored region (%) 70.4
        Additional allowed region (%) 27.1
        Generously allowed region (%) 2.1
        Disallowed region (%) 0.3

Values in parentheses are for the highest-resolution shell (3.83-3.70 Å).

Rmerge = ∑i|I(h)i — 〈I(h)〉|/∑i|I(h)i|, where 〈I(h)〉 is the mean intensity of equivalent reflections.

The last shell Rmerge is rather high as a result of strong anisotropy.

Rwork = ∑|Fo — Fc|/∑|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.

Rfree = ∑|Fo — Fc|/∑|Fo|, calculated using a test data set, 10% of total data randomly selected from the observed reflections.

r.m.s., root mean square.
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M, & Miyano M. (2008). Crystal Structure of Squid Rhodopsin with Intracellularly Extended Cytoplasmic Region. The Journal of Biological Chemistry, 283(26), 17753-17756.
Publication 2008
11-cis-Retinal Anisotropy Bos taurus Buffers Cells Centrifugation Complement Factor B concanavalin A-sepharose Crystallization DEAE-Cellulose Diffusion Disulfides Dithiothreitol dodecyldimethylamine oxide dodecyl maltoside Edetic Acid Electrostatics factor A glutamyl endopeptidase Glycol, Ethylene Helix (Snails) HEPES High-Performance Liquid Chromatographies Light Mass Spectrometry methylmannoside Microtubule-Associated Proteins Peptide Hydrolases Plant Roots polyethylene glycol 400 Proline Proteins Retina Rhodopsin Schiff Bases Sodium Chloride Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Squid Sucrose Tandem Mass Spectrometry Tissue, Membrane Todarodes Ultrafiltration X-Ray Diffraction
2
Comprehensive Oxidative Stress Biomarker Assay
Cited 6 times
All samples were assessed using a microplate reader spectrophotometer (InfiniteM200, Tecan, Austria). All the determinations were duplicated, and the interassay coefficient of variation was in the range indicated by the kit's manufacturer.
The malondialdehyde (MDA) levels were analysed spectrophotometrically using the modified thiobarbituric acid-reactive substance method to determine the amount of lipid peroxidation in plasma. The measurement of thiobarbituric acid-reactive substances (TBARS) by a commercial assay kit (Cayman Chemical, USA) allows a rapid photometric detection at 535 nm of the thiobarbituric acid malondialdehyde (TBAMDA) adduct, as previously reported [7 (link)]. A linear calibration curve was computed from pure MDA-containing reactions.
The protein carbonyl (PC) content, an index of protein oxidation, was determined utilizing a commercial kit (Cayman Chemical, USA) through the reaction of 2,4-dinitrophenylhydrazine (DNPH) and carbonyls. This reaction forms a Schiff base producing the correspondent hydrazone. The latter was analysed by spectrophotometry, reading the absorbance signal in the 360–385 nm range. Values were normalized to the total protein concentration in the final pellet (absorbance reading at 280 nm) to consider protein loss during the washing steps.
8-OH-2-deoxyguanosine (8-OH-dG), established as a marker of oxidative DNA damage, was assessed by using a commercially available enzyme immune assay EIA kit (Cayman Chemical, USA). The EIA employs an anti-mouse IgG-coated plate and a tracer consisting of an 8-OH-dG-enzyme conjugate, while the sample 8-OH-dG concentration was determined using an 8-OH-dG standard curve. Meanwhile, samples and standards were read at a wavelength of 412 nm.
Nitrite (NO2−)+nitrate (NO3−) (NOx) level determination was performed by the spectrophotometric method to Griess reagent, utilizing a commercial colorimetric assay kit (Cayman Chemical, USA).
Nitric oxide synthase (iNOS) expression was assessed by using a commercial assay EIA kit (cat no. EH0556; FineTest, Wuhan China). This assay was based on sandwich enzyme-linked immune-sorbent assay technology and carried out according to the manufacturer's instructions, while NOS2/iNOS protein synthesis was determined using a standard curve. Samples and standards were read at a wavelength of 450 nm.
Interleukin-6, interleukin-1β, and interleukin-10 (IL-6, IL-1β, and IL-10, respectively) levels were determined by using commercially available enzyme immune assay kits (R&D Systems, USA; Cayman Chemical, USA; and BioVendor, Czech Republic, respectively) following the manufacturer's instruction. The assays are based on a double-antibody sandwich technique. The signal was spectrophotometrically measured.
Mrakic-Sposta S., Montorsi M., Porcelli S., Marzorati M., Healey B., Dellanoce C, & Vezzoli A. (2022). Effects of Prolonged Exposure to Hypobaric Hypoxia on Oxidative Stress: Overwintering in Antarctic Concordia Station. Oxidative Medicine and Cellular Longevity, 2022, 4430032.
Publication 2022
8-Hydroxy-2'-Deoxyguanosine anti-IgG Biological Assay Caimans Colorimetry Deoxyguanosine dinitrophenylhydrazine Enzyme Assays Enzymes Griess reagent Hydrazones IL1B protein, human IL10 protein, human Immunoglobulins Interleukin-1 beta Lipid Peroxidation Malondialdehyde Mus Nitrates Nitric Oxide Synthase Nitric Oxide Synthase Type II Nitrites NOS2A protein, human Oxidative DNA Damage Photometry Plasma Protein Biosynthesis Proteins Schiff Bases Spectrophotometry thiobarbituric acid Thiobarbituric Acid Reactive Substances
3
Molecular Mechanics Optimization of Retinal
Cited 6 times
Molecular mechanics optimizations were performed with CHARMM76 . Since the primary focus of this study was to refine the polyene chain torsional potentials while maintaining consistency with the CHARMM protein, lipid, and water force fields, we adopted previously developed force field parameters for terms other than the torsional potential. For neutral retinal, all parameters for the β-ionone ring as well as all parameters excluding torsions for the polyene chain and deprotonated Schiff base were taken from the CHARMM General Force Field77 (link). For protonated retinal, β-ionone ring parameters were identical to neutral retinal, while for the polyene chain and PSB the internal energy parameters and atomic charges are unique to each atom, due to the delocalization of the positive charge. For these atoms we employed the parameters developed by Nina et al78 (link) that used the CHARMM force field development strategy. For both neutral and protonated retinal, we found the QM minimized energy structure was reproduced with good accuracy by the MM force field. The entire retinal force field (neutral and protonated) is included in the Supporting Information (SI).
To determine dihedral parameters, coordinate scans were carried out in CHARMM, which paralleled the QM calculations. Beginning from C5=C6–C7=C8 along the main chain each dihedral angle was examined sequentially. For the dihedral angle of interest the force constant(s) were set to zero, and the difference between the QM results and the remaining terms in the potential energy function were fit by adjustment of the force constant of each dihedral, fold number, and phase angle. A second stage of refinement was to rescan each dihedral angle using the new parameters for the other dihedrals. All of the dihedrals showed consistent results with the exception of C1–C6–C7=C8. This is because C1–C6–C7=C8 rotation involves strong steric interactions between the β-ionone ring and the polyene chain, making the C1–C6–C7=C8 and C6–C7=C8–C9 torsional parameters highly dependent on each other. Thus, C1–C6–C7=C8 and C6–C7=C8–C9 dihedrals were repeatedly parameterized until the results converged with the ab initio calculations.
Zhu S., Brown M.F, & Feller S.E. (2013). Retinal Conformation Governs pKa of Protonated Schiff Base in Rhodopsin Activation. Journal of the American Chemical Society, 135(25), 9391-9398.
Publication 2013
Ionones Lipids Mechanics Polyenes Proteins Radionuclide Imaging Retina Schiff Bases
4
Enzyme Immobilization on Aldehyde-Activated Agarose Supports
Cited 4 times
The supports were previously activated with the respective procedure and then submitted to enzyme immobilization. The glyoxyl-agarose is obtained by reaction of agarose gel in reductive-basic environment (NaOH 1.7 M, with NaBH4 28.4 mg/mL, 4 °C) with glycidol overnight, then oxidized with NaIO4 for 2 h and washed.
The agarose glutaraldehyde support was activated as previously reported [34 ], briefly the aldehyde-agarose (17.5 g) is aminated with ethylenediamine (EDA, 2 M pH 10.00) for 2 h and reduced with NaBH4 (1 g, 2 h). The EDA activated agarose was then suspended in 0.2 M phosphate buffer pH 7 (3.4 mL) and a solution of 25% (v/v) glutaraldehyde (5.1 mL) was added. The mixture was kept under stirring for 16 h at room temperature in the darkness.
Immobilization on aldehyde activated carriers was performed slightly modifying the procedure previously reported [36 (link),37 (link)]. The aldehyde-agarose gel (1.4 mL), glyoxyl agarose or agarose gluteraldehyde, were suspended in 50 mM carbonate buffer at pH 10.05. After the addition of 25 IU of protease N enzyme extract (0.5 g), the suspension (14 mL) was kept under mechanical stirring during 2.5 h. The chemical reduction of Schiff bases was carried out by adding to the mixture 14 mg of NaBH4 (1 mg/mL) over 30 min. The immobilized enzyme was then filtered and washed with 10 mM potassium phosphate buffer pH 5.0.
Bavaro T., Cattaneo G., Serra I., Benucci I., Pregnolato M, & Terreni M. (2016). Immobilization of Neutral Protease from Bacillus subtilis for Regioselective Hydrolysis of Acetylated Nucleosides: Application to Capecitabine Synthesis. Molecules, 21(12), 1621.
Publication 2016
Aldehydes Buffers Carbonates Darkness Enzymes Enzymes, Immobilized Ethylenediamines Glutaral glycidol glyoxyl agarose Immobilization Peptide Hydrolases Phosphates potassium phosphate Schiff Bases Sepharose
5
Mannosylation of HPCD-Spermine and HPCD-PEI Conjugates
Cited 3 times
To samples of 200–600 µL of HPCD-spermine and HPCD-PEI conjugates with an average concentration of 25 mg/mL and 60–200 mg/mL respectively, a one-and-a-half-fold molar excess (relative to the number of NH2-groups) of 3 M mannose water solution was added drop by drop with intensive stirring for 1 h, followed by small portions of dry Schiff base reducing agent NaBH4. Purification of conjugates from low molecular weight impurities was carried out using centrifuge filters, as described above. The purity of the preparation was controlled by HPLC gel filtration in a Knauer chromatography system (Knauer, Berlin, Germany) on BioFox 17 SEC in a 15 cm × 1 cm2 column. The eluent was 15 mM PBS (pH 7.4) containing 150 mM NaCl; the elution rate was 0.5 mL/min, 25 °C. The chromatogram of the resulting conjugate is shown in supplemental material Figure S24. The resulting conjugates were lyophilized or frozen and stored at −20 °C.
The degree of mannosylation was calculated according to spectrophotometric titration of amino groups (before and after mannosylation) with 2,4,6-trinitrobenzenesulfonic acid [28 (link)] and fluorescence analysis with orthophthalic aldehyde and 2-mercaptoethanol [80 (link),81 (link)] (Figure S25). Mainly primary amino groups are detected.
Zlotnikov I.D, & Kudryashova E.V. (2022). Spectroscopy Approach for Highly-Efficient Screening of Lectin-Ligand Interactions in Application for Mannose Receptor and Molecular Containers for Antibacterial Drugs. Pharmaceuticals, 15(5), 625.
Publication 2022
2-Mercaptoethanol Aldehydes Chromatography Fluorescence Freezing Gel Chromatography High-Performance Liquid Chromatographies Mannose Molar Reducing Agents Schiff Bases Sodium Chloride Spectrophotometry Spermine Sveinsson Chorioretinal Atrophy Titrimetry Trinitrobenzenesulfonic Acid

Most recents protocols related to «Schiff Bases»

1
Antioxidant Activity of Schiff Base-Metal Complex
Not available on PMC !

Example 4

Anti-oxidant activity

The prepared novel complex showed Antioxidant activity with an IC50 of 9.7 μg/ml against the breast cancer cell line compared with the 1-ascorbic acid standard antioxidant (IC50=55.2 μg/ml).

It is to be understood that the Schiff base-metal complex is not limited to the specific embodiments described above, but encompasses any and all embodiments within the scope of the generic language of the following claims enabled by the embodiments described herein, or otherwise shown in the drawings or described above in terms sufficient to enable one of ordinary skill in the art to make and use the claimed subject matter.

US11873313B1. Development of novel tetra nuclear distorted square anti-prism Dy (III) imine complex for pharmaceutical and industrial applications (2024-01-16). KING FAISAL UNIVERSITY [SA]. Inventors: Hany Mohamed Ab El-Lateef Ahmed [SA], Mai Mustafa Khalaf Ali [SA], Ahmed M. Abu-Dief [SA], Mohammed S. M. Abdelbaky [ES], Santiago Garcia-Granda [ES].
Patent 2024
Antioxidant Activity Antioxidants Ascorbic Acid Coordination Complexes Generic Drugs Imines MCF-7 Cells Pharmaceutical Preparations prisma Schiff Bases Tetragonopterus
2
Synthesis and Characterization of Schiff Base 1
All chemicals used were of the highest grade available and were used as received. Schiff base 1 was synthesized based on a previous report.51 The tris(2,4-dibromophenyl)aminium hexafluoroantimonate oxidant (N(C6H3Br2)3SbF6, E1/2 = 1.14 V vs. Fc/Fc+ in MeCN)52,53 (link) was prepared from commercially available triphenylamine by reported procedures.17,54 (link)1H and 13C NMR spectra were collected at Trinity Western University on a Bruker ASCEND III 400 MHz with Bruker AVANCE III 400 MHz instrument running the TopSpin 3.1.6 program. Mass spectrometry data (electrospray ionization (ESI) positive ion or ESI negative ion) were collected at Simon Fraser University on an Agilent 6210 TOF ESI-MS instrument. Elemental analyses (C, H, N) were performed at the University of British Columbia on a Thermo Flash 2000 elemental analyzer. Electronic spectra were collected on a Cary 50 spectrophotometer using a custom designed immersion fiber-optic probe with a path length of 1 mm (Hellma Inc.). Temperatures were maintained during data collection using a dry ice/acetone bath (−78 °C). Cyclic voltammetry (CV) data were collected on a CHI-630E potentiostat connected to a three electrode voltammetry cell (Ag/AgCl wire reference electrode, glassy carbon working electrode, and a Pt auxiliary electrode) with tetra-n-butylammnoiumperchlorate (nBu4NClO4, 0.1 M) as supporting electrolyte. Cobaltaceniumhexafluorophosphate (E1/2 = −1.34 V vs. Fc/Fc+ in 0.1 M nBu4NClO4 in CH2Cl2) were used as internal standards.
Sailer R., VandeVen W., Teindl K, & Chiang L. (2023). NiII and CuII complexes of a salen ligand bearing ferrocenes in its secondary coordination sphere. RSC Advances, 13(11), 7293-7299.
Publication 2023
A-A-1 antibiotic Acetone Bath Carbon Carbon-13 Magnetic Resonance Spectroscopy Cells Dry Ice Electrolytes Mass Spectrometry Oxidants Schiff Bases sodium polymetaphosphate Submersion Tetragonopterus Tromethamine
3
Synthesis of Schiff Base Chemosensors

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2023
1H NMR Amines Ethanol Ethyl Ether ethyl vanillin Figs Filtration Schiff Bases Vacuum
4
Synthesis of R-BU-CsSB and R-BU-Cs Hydrogels
A series of novel R-BU-CsSB and R-BU-Cs hydrogels has been prepared via an essential similar four-step procedure as follows:
Step 1: Benzaldehyde (20 mL) was added slowly to the Cs suspension (5 g swollen in 60 mL of MeOH for an hour) at room temperature and stirred for 24 h before being filtered. The formed yield (chitosan Schiff’s base, CsSB) was dried, after being washed several times with MeOH, for 8 h in an oven at 55 °C. This step was performed to protect the amino groups of chitosan and confine the modification reaction on the primary -OH group at C6 in chitosan [31 (link)].
Step 2: Epichlorohydrin (10 mL) was slowly added to 4 g of CsSB that was stirred in 120 mL of aqueous NaOH solution (0.001 mol L−1) at room temperature for 15 min in order to swell and alkalize. The stirring was continued for an additional 6 h, and the resulting epoxy chitosan Schiff’s base (ECsSB) was collected by filtration, rinsing it many times with water then MeOH and drying it at 55 °C [32 (link)].
Step 3: R-BU (1 mmol) was dissolved in 25 mL of EtOH and then mixed with ECsSB suspension (2.35 g, 2 mmol), which was swollen in 60 mL aqueous NaOH solution (0.001 mol L−1), and the resulting mixture was stirred at room temperature overnight. The yield, R-BU-chitosan Schiff’s base (R-BU-CsSB), was obtained through filtration, repeated washing with H2O and then MeOH, and finally drying at 55 °C.
Step 4: R-BU-CsSB (2 g) was stirred in ethanolic HCl solution (60 mL, 0.24 mol L−1) at room temperature for 24 h. Then, aqueous sodium carbonate solution (1 wt%) was used to neutralize the reaction mixture until pH 7 was reached. The resulting R-BU-chitosan (R-BU-Cs) was filtered, rinsed with water then ethanol, and dried to a constant weight at 55 °C (Scheme 2).
Alharbi R.A., Alminderej F.M., Al-Harby N.F., Elmehbad N.Y, & Mohamed N.A. (2023). Design, Synthesis, and Characterization of Novel Bis-Uracil Chitosan Hydrogels Modified with Zinc Oxide Nanoparticles for Boosting Their Antimicrobial Activity. Polymers, 15(4), 980.
Publication 2023
benzaldehyde Chitosan Epichlorohydrin Epoxy Resins Ethanol Filtration Hydrogels Schiff Bases sodium carbonate
5
Spectrophotometric Determination of Lipid Peroxidation
Colored trimetin complex with maximum absorption at a green light filter was used to determine the concentration of MDA expressed in nmol/mL of erythrocytes [21 (link)]. The results were estimated as the following:
where D—optical density, 50—dilution, 1.56—the molar extinction coefficient MDA.
The lipid peroxidation products concentration was determined by the absorption of a monochromatic light flux in the ultraviolet region of the spectrum by a lipid extract. The amount of diene conjugates (DC), triene conjugates (TC) and Schiff bases (SB) are extracted in heptane-isopropanol fractions. Measurement of optical densities (E) was performed on a SF-2000 spectrophotometer (CJSC OKB Spectrum, St. Petersburg, Russian Federation). DC, TC and SB concentration was calculated from the relative values of E232\E220, E278\E220, E400\E220 and in relative units.
Deryugina A.V., Danilova D.A., Pichugin V.V, & Brichkin Y.D. (2023). The Effect of Molecular Hydrogen on Functional States of Erythrocytes in Rats with Simulated Chronic Heart Failure. Life, 13(2), 418.
Publication 2023
Erythrocytes Extinction, Psychological Heptane Isopropyl Alcohol Light Lipid Peroxidation Lipids Molar Schiff Bases Technique, Dilution Trimetin

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Protein carbonyl colorimetric assay kit by Cayman Chemical
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More about "Schiff Bases"

Schiff bases, also known as imine compounds, are a versatile class of organic molecules formed through the condensation reaction between a primary amine and an aldehyde or ketone.
These versatile compounds play a crucial role in various biological processes, including enzyme catalysis, protein structure, and metabolic pathways.
In the field of medicinal chemistry, Schiff bases have been extensively studied for their potential therapeutic applications, such as anti-microbial, anti-cancer, and anti-inflammatory properties.
Researchers often utilize analytical techniques like the Protein Carbonyl Colorimetric Assay Kit and the Periodic Acid-Schiff (PAS) kit to investigate the structure and function of these compounds.
Schiff base formation can occur in the presence of solvents like DMSO, and reducing agents like Sodium borohydride are sometimes used to stabilize the imine bond.
Spectroscopic methods, such as the Spectrum One FTIR spectrometer, are commonly employed to characterize and identify Schiff base structures.
Beyond their medicinal applications, Schiff bases also find use in catalysis, materials science, and sensor technology.
The AI-driven platform PubCompare.ai helps researchers explore this dynamic world of Schiff bases, providing access to the best protocols from literature, preprints, and patents.
By utilizing advanced comparisons, the platform can identify the optimal products and procedures, streamlining research and maximizing results.
Whether you're investigating the role of Schiff bases in biological systems, developing novel therapeutic agents, or exploring their applications in other fields, PubCompare.ai's powerful tools can help you navigate this exciting and diverse area of chemistry.
Experience the difference that PubCompare.ai's precision and insights can make in your Schiff base investigations today.