Cumulative CAMAG Bibliography Service CCBS

Our CCBS database includes more than 11,000 abstracts of publications. Perform your own detailed search of TLC/HPTLC literature and find relevant information.

The Cumulative CAMAG Bibliography Service CCBS contains all abstracts of CBS issues beginning with CBS 51. The database is updated after the publication of every other CBS edition. Currently the Cumulative CAMAG Bibliography Service includes more than 11'000 abstracts of publications between 1983 and today. With the online version you can perform your own detailed TLC/HPTLC literature search:

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      130 141
      Two-dimensional high-performance thin-layer chromatography for the characterization of milk peptide properties and a prediction of the retention behavior – a proof-of-principle study
      M. TREBLIN, T. VON OESEN, L.-C. CLASS, G. KUHNEN, I. CLAWIN-RÄDECKER, D. MARTIN, J. FRITSCHE, S. ROHN* (*Department of Food Chemistry and Analysis, Institute of Food Technology and Food Chemistry, Technical University of Berlin, Berlin, Germany;

      J Chromatogr A 1653, 462442 (2021). Samples were peptides obtained through tryptic hydrolysis of the 5 most abundant milk proteins: α-lactalbumin (α-LA), β-lactoglobulin (β-LG), α-, β- and κ-casein (CA). As standards, synthetic whey and pea (Pisum sativum, Fabaceae) peptides (selected based on the in silico tryptic digest of α-LA, β-LG, legumin A, and vicilin with one or zero miscleavages) were only used in the last assay for prediction of the RF values of peptides with known amino-acid (AA) sequences. Two-dimensional HPTLC on silica gel (pre-washed with methanol and activated 10 min at 100°), first with basic mobile phase sec-butanol – pyridine – ammonia – water 39:34:10:26, and (after 12h drying) in the orthogonal direction with acidic mobile phase sec-butanol – pyridine – acetic acid – water 11:8:2:5. Derivatization for peptides and proteins by immersion into fluorescamine (0.05 % in acetone); visualization under UV 254 nm and 365 nm. Computer-assisted determination of the x- and y-coordinates of the derivatized zones. Repeatability (n=8) of the 2D-HPTLC was statistically tested with the Kolmogorov-Smirnov test for normal distribution and with Dixon’s Q test for outliers. Relative standard deviation (RSD) for the RF values was 12.9 % for the first dimension (y-coordinates) and 16.5 % for the second dimension (x-coordinates). According to their higher intensity and sharpness, 15 – 20 detected zones from each protein hydrolyzate were selected, manually scraped from the derivatized layer, dissolved in formic acid solution (0.1 % in acetonitrile – water 3:2), mixed with an equal volume of matrix (dihydroxybenzoic acid 2 % in acetonitrile – water 3:7), crystallized on air on a ground steel target, before being desorbed by the laser beam of the MALDI-TOF-MS/MS (matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry). Direct hyphenation of HPTLC to MS was not performed, to avoid zone diffusion during plate coating with the matrix and to circumvent the stronger binding of polar peptides on the layer.  The MS spectra were acquired in positive reflector mode in m/z range 340 – 4000 (10 – 2500 for fragments), using an external peptide as calibration standard. Identification of 51 from the 85 selected peptides according to AA sequences was performed, using software programs allowing m/z calculation of protein fragments and estimation of cleavage sites. Correlation of the retention behaviour of the peptides with their properties (molecular weight MW, isoelectric point IEP, charges, polarity) was tested with Student’s two-sided t-test after calculation of Pearson’s correlation coefficients. The correlation was significant with IEP, percentages of anionic AA and of non-polar AA; but not with the following properties: MW, percentages of cationic AA and of uncharged polar AA. Finally, based on the correlation results, regression formulas were found to calculate the x- and y-coordinates of any known peptide from the percentage of non-polar AA (or vice-versa). The prediction power of these formulas was verified by repeating the complete 2D-HPTLC-MS experiment with the standard peptides of whey and of peas, and measuring the absolute and relative deviations between the actual x- and y-coordinates and the predicted values. The absolute deviations were higher in the lower RF zones. The average, relative RF value deviations (range 22.1 – 25.7 %) were not different between whey and pea peptides.

      Classification: 2c, 2d, 4e, 18b, 19, 32e
      130 147
      Globotriaosylceramide-related biomarkers of Fabry disease identified in plasma by high-performance thin-layer chromatography – densitometry – mass spectrometry
      C. JARNE, L. MEMBRADO, M. SAVIRÓN, J. VELA, J. ORDUNA, R. GARRIGA, J. GALBÁN, V. L. CEBOLLA* (*Institute of Carbon Chemistry, Spanish National Research Council (CSIC), Saragossa, Spain;

      J Chromatogr A 1638, 461895 (2021). Samples were sphingolipid-rich fractions of unproteinated blood plasma from healthy humans or from Fabry’s disease patients, as well as standards of sphingomyelin (SM) and of globotriaosylceramides (Gb3 = ceramide trihexosides), and related compounds (lyso-ceramide trihexosides, lactosyl ceramide, glucosyl ceramide). HPTLC on silica gel (Lichrosphere with spherical particles) by automated multiple development with a 9-step gradient, starting with pure methanol and ending with dichloromethane – methanol 9:1. Visualization and densitometry under UV 190 nm. Derivatization for Gb3 and derivatives (but not for SM) by immersion into orcinol solution (0.2 %, with sulfuric acid 10 %), followed by 15 min heating at 100 °C and by densitometry under visible light 550 nm. Bands of interest were directly eluted with methanol from underivatized plates into an ion-trap MS, through the oval head of a TLC-MS interface (with stainless steel frit to remove silica gel particles). Two different ionization processes were used: (A) electrospray ionization (ESI, capillary voltage 4 kV, endplate offset voltage -0.5 kV, nebulizer pressure 40 psi, drying gas 9 mL/min at 350 °C); (B) atmospheric pressure chemical ionization (APCI, capillary voltage 2–3 kV, current intensity 4.5 µA, nebulizer pressure 45 psi, drying gas 5 mL/min at 350 °C; vaporization at 450 °C). Full MS spectra were recorded up to m/z 1500 in positive ion mode. The relative ion intensities were used to quantify the detected species. Previous to this study, the precision of the elution head positioning was tested on Gb3 standard zones, comparing 3 positions for analyte elution: from the centre and from each higher or lower side of the band. The same main m/z peaks were observed in the 3 positions, but in different proportions. This was explained by the presence of coeluting Gb3 subclasses (the ceramide moiety CM being either saturated, mono-unsaturated fatty acyl with a slightly higher migration distance, or polar hydroxyl fatty acyl with the opposite effect on migration) and of coeluting Gb3 isoforms (the hexoside moiety consisting of glucose and/or galactose units). This resulted in the broadening and partial splitting of the standard band. In the plasma samples, 19 molecular species of Gb3 were identified (depending on the CM, the sugar isoforms being undistinguishable by MS): 5 with a saturated CM, 7 with two additional double bonds on the CM, 7 with a methylated CM. In case of Fabry’s disease, most Gb3 species with saturated CM were highly increased, whereas other species were decreased.

      Classification: 4e, 11c, 11e, 32f
      130 146
      Development of a thin-layer chromatography bioautographic assay for neuraminidase inhibitors hyphenated with electrostatic field induced spray ionisation-mass spectrometry for identification of active Isatis indigotica root compounds
      Y. ZANG (Zang Yichao), Y. MIAO (Miao Yu), T. WU (Wu Tao)*, Z. CHENG (Cheng Zhihong)** (*Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, China,; **Department of Natural Medicine, School of Pharmacy, Fudan University, Shanghai, China,

      J Chromatogr A 1638, 461597 (2021). Samples were Isatis tinctoria (= I. indigotica) root extracts (Brassicaceae) and their fractions. Standards were oseltamivir acid (OA), a neuraminidase (NA) inhibitor; pinoresinol (PR, a lignan), β-sitosterol (SS, a sterol), and dihydro-neoascorbigen (DHNA, an alkaloid). HPTLC / TLC on silica gel with (1) petroleum ether – ethyl acetate – acetic acid 48:8:1 for petroleum ether extracts and SS, or 30:40:1 for ethyl acetate extracts, or 10:30:1 for PR; (2) with toluene – ethyl acetate – methanol – formic acid 16:3:1:2 or 10:4:1:2 also for ethyl acetate extracts and DHNA; (3) with n-butanol – acetic acid – water 25:4:3 for butanol extracts. OA was applied but not developed. RP-18, polyamide, cellulose, alumina layers were tested, but the resolution was lower. Derivatization by spraying with sulfuric acid (10 % in ethanol). Enzymatic assay by immersion of the plates into neuraminidase solution (6 U/mL), followed by 1 h incubation at 37 °C and by immersion into chromogenic substrate solution (1.75 mM 5-bromo-4-chloro-3-indolyl-α-D-N-acetylneuraminic acid). After 5 min, NA inhibitors were seen as white zones on blue background. The experiment was previously improved for the following parameters: incubation times, substrate and enzyme concentrations, followed by statistical evaluation and calculations using Box-Behnken design. Quantification by absorbance measurement (detection wavelength 605 nm, reference wavelength 420 nm). In optimal conditions, OA had LOD 300 ng/zone. Zones of interest on underivatized plates were directly submitted to MS, using EFISI (electrostatic-field-induced spray ionisation), as follows. Chromatograms were immersed 1–3 s into dimethicone – n-hexane 1:1 to form a hydrophobic film, and dried 30 min at room temperature; on the analyte spot, a hydrophilic droplet was formed with 5 µL methanol – water 1:1, extracting the analyte from the layer; the analyte was further attracted through a capillary tube (3–4 cm long, made of non-deactivated fused silica) under a strong electrostatic field, into the in-let orifice of the triple-quadrupole ­– linear ion-trap MS (induction voltage 4 kV; capillary voltage 40 V; tube lens voltage 100 V; capillary temperature 200 °C). Full-scan spectra were recorded in m/z range 50 – 1000, helium was used for collision-induced dissociation. 11 active compounds were identified in the extract: SS, 6 alkaloids (including cycloanthranilylproline, DHNA, hydroxy-indirubin, isatindigodiphindoside, isatindinoline A and), 3 lignans (including PR and isolariciresinol), 1 fatty acid (trihydroxy-octadecenoic acid).

      Classification: 4e, 8a, 8b, 11a, 13c, 22
      130 149
      HPTLC/HPLC-mass spectrometry identification and NMR characterization of major flavonoids of wild lemongrass (Cymbopogon giganteus) collected in Burkina Faso
      R.K. BATIONO*, C.M. DABIRÉ, A. HEMA, R.H.CH. NÉBIÉ, E. PALÉ, M. NACRO (*Laboratory of Applied Organic Chemistry and Physics, Joseph Ki-Zerbo University, Ouagadougou, Burkina Faso;

      Heliyon 8(8), e10103 (2022). Samples were a methanolic extract of Cymbopogon giganteus leaves (= C. caesius subsp. giganteus, Poaceae), as well as flavones as standards: isorhamnetin, luteolin and orientin (=luteolin 8-C-glucoside). HPTLC on silica gel with ethyl acetate – acetic acid – formic acid – water 100:11:11:26. Derivatization for flavones with Neu’s reagent (ethanolamine diphenylborate – PEG). Visualization under UV 365 nm. The standards (hRF 75, 70-72 and 96, respectively) were not detected in the extract. Some analytes detected by the reagent were scraped from the underivatized plate into a tube, and injected through a TLC-MS interface into a double-quadrupole – time-of-flight MS (electrospray ionization). Full mass scan spectra were recorded in positive and negative ionization modes in m/z range 150–550. For 3 of the compounds, isolated through MPLC columns, the HPTLC-MS results, combined to the NMR and HPLC-MS analyses, allowed the identification as epicatechin (hRF 86, a flavanol, not coloured by Neu’s reagent) and as luteolin 8-C- and 6-C-glucosides (hRF 67-70).

      Classification: 4e, 8a, 32e
      130 048
      Coding recognition of the dose–effect interdependence of small biomolecules encrypted on paired chromatographic‑based microassay arrays
      Y. DENG* (Deng Yifeng), Z. LIN (Lin Zhenpeng), Y. CHENG (Cheng Yuan) (*Guangdong Key Laboratory for Research & Development of Natural Drugs, Guangdong Medical University, Zhanjiang 524023, China,

      Anal. Bioanal. Chem. 414, 5991-6001 (2022). 2D-HPTLC fingerprint of Alpinia officinarum on silica gel in 384-well microplate array format (4.5 × 4.5 mm) matrix with trichloromethane - methanol - petroleum ether 97:3:25 in the first dimension and ethyl acetate - petroleum ether - acetic acid 15:35:1 in the second dimension. The paired chromatographic-based microassay array with the consistent chromatographic distribution was prepared by transferring a portion of the sample from the stock chromatographic-based microassay arrays to the corresponding array units of another 384-well microplate. A G‑quadruplex ligand bioassay was used to evaluate the ligand activity of the components in each array unit of the chromatographic-based microassay array. Further analysis by mass spectrometry. 

      Classification: 4e
      130 049
      Quantitative detection of caffeine in beverages using flowing atmospheric‑pressure afterglow (FAPA) ionization high‑resolution mass spectrometry imaging and performance evaluation of different thin‑layer chromatography plates as sample substrates
      M. HEIDE, C. ESCOBAR, C. ENGELHARD* (*Department of Chemistry and Biology, University of Siegen, Adolf-Reichwein-Str. 2, 57076 Siegen, Germany,

      Anal. Bioanal. Chem. 414, 4481-4495 (2022). HPTLC of selected caffeine-containing standards and beverages (Red Bull, Coca-Cola, coffee, and black tea) on different stationary phases (silica gel, RP- and cyano-) with propan-2-ol - n-heptane - water 7:3:1. Direct surface analysis of the TLC plates with a flowing atmospheric pressure afterglow (FAPA) ambient desorption/ionization source (TLC-FAPA-MS). CN-HPTLC plates were the most efficient stationary phase, resulting in a significantly more intense caffeine signal.

      Keywords: food analysis HPTLC
      Classification: 4e
      130 030
      High-performance thin-layer chromatography hyphenated with microchemical and biochemical derivatizations in bioactivity profiling of marine species
      Snezana AGATONOVIC-KUSTRIN*, E. KUSTRIN, V. GEGECHKORI, D. W. MORTON (*Department of Pharmaceutical and Toxicological Chemistry, Institute of Pharmacy, Sechenov University, Moscow, Russia, and School of Pharmacy and Biomedical Sciences, La Trobe Institute for Molecular Sciences, La Trobe University, Bendigo, Australia;

      Marine Drugs 17(3), 148 (2019). Samples were ethyl acetate extracts of seagrass Amphibolis antarctica (Cymodoceaceae), and of algae: Austrophyllis harveyana (Kallymeniaceae), Carpoglossum confluens, Cystophora harveyi, C. monilifera, C. pectinata and C. subfarcinata, Myriodesma integrifolium, Sargassum lacerifolium (Sargassaceae), Codium fragile subsp. tasmanicum (Codiaceae), Ecklonia radiata (Lessoniaceae), Hypnea valida, Rhodophyllis membaneacea (Cystocloniaceae), Hormosira banksii (Hormosiraceae), Perithalia caudata (Sporochnaceae), Phyllospora comoasa, Scytothalia dorycarpa (Seirococcaceae), Plocamium dilatatum (Plocamiaceae), and epiphytic brown algae. HPTLC on silica gel (pre-washed with methanol and heated 30 min at 100 °C) with n-hexane – ethyl acetate – acetic acid 15:9:1. Derivatization by immersion: A) into anisaldehyde – sulfuric acid reagent, followed by 10 min heating at 105 °C, for the detection of steroids and terpenes; B) into DPPH• (0.2 % in methanol), followed by 30 min incubation in the dark, for the detection of antioxydants; C) into Fast Blue B solution (0.1 % in 70 % ethanol) for detection of phenols (with alkylresorcinols detected as dark purple zones on colorless background). Effect-directed analyses were performed directly on the plates. D) α-Amylase inhibition assay by immersion into enzyme solution, incubation 30 min at 37 °C, immersion into substrate solution (starch 2 % in water), incubation 20 min at 37 °C and immersion into Gram’s iodine solution for detection (inhibition zones appear blue on white background). E) Acetylcholinesterase (AChE) inhibition assay (after neutralization by immersion into phosphate buffer) by immersion into enzyme solution, incubation 30 min at 37 °C, immersion into substrate solution (α-naphthyl acetate) and into dye reagent (Fast Blue Salt B). Densitometry through automated scanning, quantification expressed as equivalents to the respective standards used for calibration curves: A) β-sitosterol (LOQ 1.6 µg/band), B) gallic acid (LOQ 60 ng/band), D) acarbose (LOQ 173 µg/band), E) donepezil (LOQ 96 µg/mL). Alkylresorcinols were detected as antioxydant in C. harveyi and C. pectinata (hRF 88), and in C. subfarcinata (hRF 72, 81, 88). Enzymatic inhibitors in C. fragile were considered as a flavone (hRF 65) and a terpenoid (hRF 77), due to their absorption curves (densitometric scan in range 200-400 nm).

      Classification: 4e, 7, 8a, 15a, 32e
      130 003
      Purification and characterization of a novel endolytic alginate lyase from Microbulbifer sp. SH-1 and its agricultural application
      J. YANG, D. CUI, D. CHEN, W. CHEN, S. MA, H. SHEN* (*College of Natural Resources and Environment, South China Agricultural University, Guangzhou, and Guangdong Provincial Key Laboratory of Eco-Circular Agriculture, Guangzhou, China;

      Marine Drugs 18(4), 184 (2020). A new alginate lyase (AlgSH7), isolated from marine bacterium Microbulbifer sp. strain SH1 (Alteromonadaceae), was incubated (24 h at 40 °C) with sodium alginate from brown algae (1 % in TRIS-HCl buffer, pH 9), or with related mannuronate and guluronate polymers (polyM and polyG), or with related saccharides with different polymerisation degrees (PD 1 – 4). TLC of reaction products as well as saccharides, on silica gel with n-butanol ­– acetic acid – water 3:2:2. Derivatization by spraying sulfuric acid (10 % in ethanol), followed by 5 min heating at 130 °C. The enzyme was active only on alginate and on polyM, cleaving them into oligomeric fragments (PD 2 – 4); it was inactive on polyG or on oligomers.

      Classification: 4e, 10