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; rohn@tu-berlin.de)

      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
      130 089
      Advances in analytical techniques coupled to in vitro bioassays in the search for new peptides with functional activity in effect-directed analysis
      Luz GUERRA*, J. PAVON, A. VALLEJOS, D. JORQUERA (*Department of Food Science and Technology, Faculty of Pharmacy, University of Concepcion, Chile, lguerra@udec.cl)

      Food Chem. 133784 (2022). Review of enzymatic protein hydrolysis, including standard and conventional techniques and their applications and insights into new strategies of detection and characterization of bioactive peptides. The paper described HPTLC methods coupled with bioassays in effect-directed analysis (EDA) to detect the bioactivities of peptides.

      Keywords: HPTLC review
      Classification: 18b
      129 070
      Effect-directed screening of Bacillus lipopeptide extracts via hyphenated high-performance thin-layer chromatography
      M. JAMSHIDI-AIDJI, I. DIMKIC, P. RISTIVOJEVIC, S. STANKOVIC, Gertrud E. MORLOCK* (*Institute of Nutritional Science, and Interdisciplinary Research Centre for Biosystems, Land Use and Nutrition, Justus Liebig University Giessen, Giessen, Germany; gertrud.morlock@uni-giessen.de)

      J Chromatogr A, 1605, 460366 (2019). Samples were standards and complex mixtures of non-ribosomally synthesized cyclic lipopeptides (CLPs) from Bacillus strains (Bacillaceae) found in soil or in manure: B. amyloliquefaciens (SS-12.6, SS-13.1, SS-27.2, SS-38.4) and B. pumilus (SS-10.7). Two extraction methods were compared: ethyl acetate extraction (Ex1), and the acidic precipitation followed by methanol extraction (Ex2). HPTLC on silica gel with chloroform – methanol – water 65:25:4. Detection under white light, UV 254 nm and 366 nm. Absorption densitometry measured at 190 nm. Derivatization for peptides, amino acids and amino derivatives, by immersion into ninhydrin – collidine reagent (ninhydrin 0.3 %, collidine 5 %, acetic acid 5 %, in ethanol), followed by heating 5 min at 110 °C. Effect-directed analysis using automated immersion: A) for free radical (DPPH•) scavengers; B) for enzymatic inhibition (acetyl-cholinesterase, α-glucosidase); C) for activity against Gram-negative (Aliivibrio fischeri bioluminescence assay) or Gram-positive bacteria (Bacillus subtilis bioassay). Active bands were eluted with methanol through the oval elution head of a TLC-MS interface pump, into a quadrupole-Orbitrap mass spectrometer. Full scan mass spectra (m/z 200−2000) in positive and in negative ionization modes were recorded using heated electrospray ionization (HESI, spray voltage 3.5 kV, capillary temperature 270 °C). Active zones were assigned to be CLPs: iturin A, surfactin dimethyl-ester, and surfactin, fengycin and kurstakin homologues. Ex1 provided richer extracts compared to Ex2. Standards were seen to contain a free radical scavenging impurity.

      Classification: 4e, 8b, 18b, 23e
      58 081
      Thin-layer chromatographic separation of stereoisomeric dipeptides
      K. GUENTHER, J. MARTENS, M. SCHICKEDANZ

      Angew. Chem. Int. Ed. Engl. 25

      Classification: 3b, 18b
      62 127
      Synthesis, conformation and immunosuppressive activity of a conformationally restricted cyclosporine lactam analogue
      J.D. AEBI*, D. GUILLAUME, B.E. DUNLAP, D.H. RICH, (*Univ. of Wisconsin, School of Pharmacy, 425 N. Charter St., Madison, Wisconsin 53706, USA)

      J. of Medicinal Chemistry 31, 1805-1815, (1988). TLC of cyclosporine A (CsA, 1) on silica with 40% acetone in hexane. Visualization with 7% phosphomolybdic acid in ethanol.

      Classification: 18b
      63 105
      Synthesis and radioprotective activity of dipeptide cysteamine and cystamine derivatives
      J. OIRY*, J.Y. PUE, J.L. IMBACH, M. FATOME, H.S. ROUMANON, (*Lab. de Chimie Bio-Organique, U. A. 488 du CNRS, 34060 Montpellier-Cédex, France)

      J. of Medicinal Chemistry 32, 297-301 (1989). TLC of N- (dipeptidyl)-S-acetylcysteamine and N, N’- (dipeptyl)cystamine on silica. Detection under UV, exposure to iodine vapor or spraying with ninhydrin.

      Classification: 17a, 18b
      67 125
      Synthesis of immunomodulatory peptides with histidine in central position
      P. PALVÖLGYI*, M. SZEKERKE, (*Institute of Organic Chemistry, Eötvös Lóránt University, H-1518 Budapest 112, P.O. Box 32, Hungary)

      Acta Chimica, 127, 569-579 (1990). TLC of the chemotactic peptides on silica with chloroform - methanol 1:9, butanol - acetic acid - water 4:1:1, pyridine - acetic acid - water - ethyl acetate 20:6:11:333 or 20:6:11:56. Detection by spraying with ninhydrin, chlorine-o-tolidine or Pauly’s reagent.

      Classification: 18b
      78 187
      Electrophoretic separation of bA4-peptides (1-40) and (1-42)
      H.W. KLAFKI, J. WILTFANG, M. STAUFENBIEL*, (*Preclin. Res., Sandoz Pharma Ltd., CH-4002 Basel, Switzerland)

      Anal. Biochem. 237, 24-29 (1996). Separation with different sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Clear resolution by addition of 8 M urea to the gel and use of a multiphasic buffer system employing bicine and sulfate as trailing and leading ions, respectively. Discussion of the migration of the peptides. Demonstration of the usefulness of the system for the analysis of the title compounds generated during cellular metabolism by immunolabeled peptides secreted by cell transfected with a myloid precursor protein CDOAS.

      Classification: 18b, 36