Slow isomerization of some proline-containing peptides inducing peak splitting during reversed-phase high-performance liquid chromatography

Gesquière, Jean‐Claude; Diesis, Eric; Cung, Manh Thông; Tartar, André

doi:10.1016/0021-9673(89)90010-1

Cited by 56 publications

(34 citation statements)

References 7 publications

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“…Surprisingly, about 40% of the protein binds the peptide with K d = 1.5nM while the other 60% binds with K d = 140 nM. We postulate that the PPKRIAKRRS peptide shows this behavior due to very slow isomerization of cis / trans peptide bond in amino acid sequences containing Pro-Pro dipeptide, as has been reported previously 16–18 . The SPKRIAKRRS peptides (both non-methylated and methylated forms) did not show biphasic binding.…”

Section: Resultssupporting

confidence: 76%

Substrate Specificity of Mammalian N-Terminal α-Amino Methyltransferase NRMT

Petkowski

Tooley

Anderson³

et al. 2012

Biochemistry

130

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N-terminal methylation of free α-amino-groups is a post-translational modification of proteins that has been known for 30 years but has been very little studied. In this modification, the initiating M residue is cleaved and the exposed α-amino group is mono- di- or trimethylated by NRMT, a recently identified N-terminal methyltransferase. Currently, all known eukaryotic α-aminomethylated proteins have a unique N-terminal motif, M-X-P-K, where X is A, P, or S. NRMT can also methylate artificial substrates in vitro in which X is G, F, Y, C, M, K, R, N, Q or H. Methylation efficiencies of N-terminal amino acids are variable with respect to the identity of X. Here we use in vitro peptide methylation assays and substrate immunoprecipitations to show that the canonical M-X-P-K methylation motif is not the only one recognized by NRMT. We predict that N-terminal methylation is a widespread post-translational modification, and that there is interplay between N-terminal acetylation and N-terminal methylation. We also use isothermal calorimetry experiments to demonstrate that NRMT can efficiently recognize and bind to its fully methylated products.

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Section: Resultssupporting

confidence: 76%

Substrate Specificity of Mammalian N-Terminal α-Amino Methyltransferase NRMT

Petkowski

Tooley

Anderson³

et al. 2012

Biochemistry

130

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“…His group estimated isomerization rate constants and the activation barrier of some proline-containing dipeptides by computer-supported Damköhler analysis, a method that is commonly used in chemical engineering. Krauss et al [12][13][14][15] and Gesquiere et al [16] also found isomerization of prolinecontaining peptides taking place on different stationary phases in HPLC and Thomas et al [17], Wüthrich et al [18], and Moroder et al [19] in NMR studies.…”

Section: Enalaprilat (1-[n-[(s)-1-carboxy-3-phenylpropyl]-l-alanyl]-mentioning

confidence: 94%

Determination of the cis‐trans isomerization barrier of enalaprilat by dynamic capillary electrophoresis and computer simulation

Trapp

Schurig

2004

Electrophoresis

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Dynamic capillary electrophoresis (DCE) and computer simulation of the elution profiles with the stochastic model has been applied to determine the isomerization barriers of the angiotensin converting enzyme inhibitor enalaprilat. The separation of the rotational cis-trans isomeric drug has been performed in an aqueous 20 mM borate buffer at pH 9.3. Interconversion profiles featuring plateau formation and peak broadening were observed. To evaluate the rate constants k(cis-->trans) and k(trans-->cis) of the cis-trans isomerization from the experimental electropherograms obtained by dynamic capillary electrophoresis, elution profiles were analyzed by a simulation with iterative convergence to the experimental data using the ChromWin software which requires the total migration times of the individual isomers t(R), the electroosmotic break-through time t(0), the plateau height h(plateau), the peak widths at half height of the individual isomers w(h), as well as the peak ratio of the isomers as experimental data input. From temperature-dependent measurements between 0 degrees and 15 degrees C the thermodynamic parameters Delta G, Delta H and Delta S, the rate constants k(cis-->trans) and k(trans-->cis) and the kinetic activation parameters Delta G*, Delta H*, and Delta S* of the cis-trans isomerization of enalaprilat were obtained. From the activation parameters the isomerization barriers at 37 degrees C were calculated to be Delta G* (trans-->cis) = 87.2 kJ.mol(-1) and Delta G*(cis-->trans) = 91.9 kJ.mol(-1).

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“…The same group estimated isomerization rate constants and the activation barrier of some proline containing dipeptides by computer aided Damkohler analysis, a method which is commonly used in chemical engineering. Krauss et al [38][39][40][41] and Gesquiere et al [42] also found isomerization of proline-containing peptides taking place on different stationary phases in HPLC, and Thomas and Williams [43], Grathwohl and Wütherich [44], and Moroder et al [29] in NMR studies.…”

Section: Introductionmentioning

confidence: 95%

Determination of thecis-trans isomerization barrier of severalL-peptidyl-L-proline dipeptides by dynamic capillary electrophoresis and computer simulation

2001

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Dynamic capillary electrophoresis (DCE) and computer simulation of the elution profiles with the theoretical plate and the stochastic model has been applied to determine the isomerization barriers of the three dipeptides L-alanyl-L-proline, L-leucyl-L-proline, and L-phenylalanyl-L-proline. The separation of the rotational cis-trans isomers has been performed in an aqueous 70 mM borate buffer at pH 9.5. Interconversion profiles featuring plateau formation and peak broadening were observed. To determine the rate constants k1 and k(-1) of the cis-trans isomerization in dynamic capillary electrophoresis, equations have been derived for the theoretical plate model and stochastic model. The electropherograms were simulated with the ChromWin software which uses the experimental data plateau height h(plateau), peak width at half height Wh, the total migration times of the cis-trans isomers tR and the electroosmotic break-through time t0 as well as the peak ratio [cis]/[trans]. From temperature-dependent measurements, the rate constants k1 and k(-1) and the kinetic activation parameters deltaG#, deltaH# and deltaS# of the cis-trans isomerization of the three dipeptides were obtained.

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Slow isomerization of some proline-containing peptides inducing peak splitting during reversed-phase high-performance liquid chromatography

Cited by 56 publications

References 7 publications

Substrate Specificity of Mammalian N-Terminal α-Amino Methyltransferase NRMT

Substrate Specificity of Mammalian N-Terminal α-Amino Methyltransferase NRMT

Determination of the cis‐trans isomerization barrier of enalaprilat by dynamic capillary electrophoresis and computer simulation

Determination of thecis-trans isomerization barrier of severalL-peptidyl-L-proline dipeptides by dynamic capillary electrophoresis and computer simulation

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