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Open-tubular capillary electrochromatography with bare gold nanoparticles-based stationary phase applied to separation of trypsin digested proteins
Mikšík, Ivan ; Lacinová, Kateřina ; Zmatlíková, Zdeňka ; Sedláková, Pavla ; Král, V. ; Sýkora, D. ; Řezanka, P. ; Kašička, Václav
Open-tubular capillary electrochromatography (OT-CEC) using bare gold nanoparticles-based stationary phase has been applied to separation of tryptic peptide fragments of native and glycated proteins, bovine serum albumin and human transferrin. OT-CEC with bare gold nanoparticles stationary phase was found to be a suitable technique for separation of complex peptide mixtures originating from enzymatic (tryptic) digestion of native and glycated bovine serum albumin and human transferrin, and for glycation studies of these proteins.
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Analysis of antimicrobial peptides by capillary electrophoresis
Ehala, Sille ; Niederhafner, Petr ; Čeřovský, Václav ; Řezanka, P. ; Sýkora, D. ; Král, V. ; Kašička, Václav
Capillary electrophoresis was used for the purity degree determination of new antimicrobial peptides: octadecapeptide melectin and tetradecapeptide mastoparan PDD-B, and their synthetic analogues. Besides, four semiempirical models correlating electrophoretic mobilities of these peptides with their charge and size (relative molecular mass) were applied to predict their probable structures in solution. Additionally, capillaries coated with gold nanoparticles were employed for the separation of mixtures of antimicrobial peptides.
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Capillary electrophoresis applied to analysis and characterization of mono-N-acyl-2,6-diaminopimelic acid derivatives
Vítovcová, M. ; Hlaváček, Jan ; Pícha, Jan ; Vaněk, Václav ; Jiráček, Jiří ; Kašička, Václav
Capillary zone electrophoresis and micellar electrokinetic chromatography have been employed for determination of electrophoretic purity degree, limit of detection and limit of quantification of twelve mono-Nacylated derivatives of 2,6-diaminopimelic acid (DAP). In addition, the DAP derivatives were characterized by effective electrophoretic mobilities of their cationic and anionic forms in several classical and isoelectric buffer-based background electrolytes within a broad pH range 2.18 – 8.64.
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Capillary electrophoresis employed for quantitative characterization of peptide interactions with small ions and cyclodextrins
Kašička, Václav ; Ehala, Sille ; Šolínová, Veronika ; Schimperková, Tereza ; Sázelová, Petra ; Koval, Dušan ; Makrlík, E.
Capillary affinity electrophoresis has been applied to investigate quantitatively two types of non-covalent peptide interactions: i) complexes of pseudopeptide valinomycin with ammonium ion and alkali metal ions, Li+, Na+, K+, Rb+ and Cs+, in methanol, and ii) complexes of enantiomers of dipeptide beta alanyl-D,L-tyrosine and its derivatives with chiral selector, 2-hydroxypropyl-beta-cyclodextrin, in water.
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