AustralieFrV1, Main, Exploration, bibRecord, 00D763

Further studies into the Boc/solid‐phase synthesis of Ser(P)‐ and Thr(P)‐containing peptides

Identifieur interne : 00D763 ( Main/Exploration ); précédent : 00D762; suivant : 00D764

Further studies into the Boc/solid‐phase synthesis of Ser(P)‐ and Thr(P)‐containing peptides

Auteurs : John W. Perich [France] ; Evelyne Terzi [France] ; Eric Carnazzi [France] ; Rene Seyer [France] ; Elisabeth Trifilieff [France]

Source :

International Journal of Peptide and Protein Research [ 0367-8377 ] ; 1994-10.

RBID : ISTEX:C7C9A9F164343CCABD3B403176708714F0773C4E

Descripteurs français

Wicri :
- topic : Spectrométrie.

English descriptors

Abstract

The Ser(P)‐containing peptide corresponding to phospholamban 11‐19, Ac‐Ala‐Ile‐Arg‐Are‐Ala‐Ser(P)‐Thr‐Ile‐Glu‐NH2, was prepared by the use of Boc‐Ser(PO3Ph2)‐OH in Boc/solid‐phase peptide synthesis followed by HF cleavage of the peptide from the polystyrene resin and subsequent platinum‐mediated hydrogenolytic cleavage of the phenyl phosphate groups. A study of the HF deprotection step showed that extensive dephosphorylation of the Ser(PO3Ph2)‐residue occurred using three commonly used HF conditions and gave rise to large quantities of the Ser‐containing peptide. The subsequent study of model peptide systems under standard HF conditions established firstly that the extent of dephosphorylation was dependent on the HF‐contact time, and secondly that the Ser(PO3Ph2) residue underwent dephosphorylation at a slightly higher rate than the Thr(PO3Ph2) residue. © Munksgaard 1994.

Url:

https://api.istex.fr/document/C7C9A9F164343CCABD3B403176708714F0773C4E/fulltext/pdf

DOI: 10.1111/j.1399-3011.1994.tb01013.x

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<author><name sortKey="Carnazzi, Eric" sort="Carnazzi, Eric" uniqKey="Carnazzi E" first="Eric" last="Carnazzi">Eric Carnazzi</name>
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<author><name sortKey="Seyer, Rene" sort="Seyer, Rene" uniqKey="Seyer R" first="Rene" last="Seyer">Rene Seyer</name>
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<author><name sortKey="Trifilieff, Elisabeth" sort="Trifilieff, Elisabeth" uniqKey="Trifilieff E" first="Elisabeth" last="Trifilieff">Elisabeth Trifilieff</name>
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<term>Amino acids</term>
<term>Analytical hplc</term>
<term>Anisole</term>
<term>Anisole acylated</term>
<term>Ch3cn</term>
<term>Cleavage</term>
<term>Complex phosphopeptides</term>
<term>Contact time</term>
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<term>Deprotection step</term>
<term>Diethyl</term>
<term>Diethyl ether</term>
<term>Early eluting product</term>
<term>Eluting product</term>
<term>Ether</term>
<term>Extensive dephosphorylation</term>
<term>Flow rate</term>
<term>Fluoride</term>
<term>Gravity filtration</term>
<term>Hplc</term>
<term>Hplc trace</term>
<term>Hydrogen fluoride</term>
<term>Hydrogen fluoride conditions</term>
<term>Hydrogen fluoride deprotection</term>
<term>Linear gradient</term>
<term>Major fractions</term>
<term>Mass spectrometry</term>
<term>Mass spectrum</term>
<term>Matrix support</term>
<term>Minutes figure</term>
<term>Mmol</term>
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<term>Peptide synthesis</term>
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<term>Polymer support</term>
<term>Positive mode</term>
<term>Preparative magnum</term>
<term>Residue</term>
<term>Simple phosphopeptides</term>
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<term>Anisole</term>
<term>Anisole acylated</term>
<term>Ch3cn</term>
<term>Cleavage</term>
<term>Complex phosphopeptides</term>
<term>Contact time</term>
<term>Dephosphorylated peptide</term>
<term>Dephosphorylation</term>
<term>Deprotection</term>
<term>Deprotection step</term>
<term>Diethyl</term>
<term>Diethyl ether</term>
<term>Early eluting product</term>
<term>Eluting product</term>
<term>Ether</term>
<term>Extensive dephosphorylation</term>
<term>Flow rate</term>
<term>Fluoride</term>
<term>Gravity filtration</term>
<term>Hplc</term>
<term>Hplc trace</term>
<term>Hydrogen fluoride</term>
<term>Hydrogen fluoride conditions</term>
<term>Hydrogen fluoride deprotection</term>
<term>Linear gradient</term>
<term>Major fractions</term>
<term>Mass spectrometry</term>
<term>Mass spectrum</term>
<term>Matrix support</term>
<term>Minutes figure</term>
<term>Mmol</term>
<term>Mobile phase</term>
<term>Monophenyl peptide</term>
<term>Peptide</term>
<term>Peptide assembly</term>
<term>Peptide prorein</term>
<term>Peptide synthesis</term>
<term>Perich</term>
<term>Phenyl</term>
<term>Phenyl group</term>
<term>Phenyl phosphate groups</term>
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<term>Preparative magnum</term>
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<front><div type="abstract" xml:lang="en">The Ser(P)‐containing peptide corresponding to phospholamban 11‐19, Ac‐Ala‐Ile‐Arg‐Are‐Ala‐Ser(P)‐Thr‐Ile‐Glu‐NH2, was prepared by the use of Boc‐Ser(PO3Ph2)‐OH in Boc/solid‐phase peptide synthesis followed by HF cleavage of the peptide from the polystyrene resin and subsequent platinum‐mediated hydrogenolytic cleavage of the phenyl phosphate groups. A study of the HF deprotection step showed that extensive dephosphorylation of the Ser(PO3Ph2)‐residue occurred using three commonly used HF conditions and gave rise to large quantities of the Ser‐containing peptide. The subsequent study of model peptide systems under standard HF conditions established firstly that the extent of dephosphorylation was dependent on the HF‐contact time, and secondly that the Ser(PO3Ph2) residue underwent dephosphorylation at a slightly higher rate than the Thr(PO3Ph2) residue. © Munksgaard 1994.</div>
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Further studies into the Boc/solid‐phase synthesis of Ser(P)‐ and Thr(P)‐containing peptides

Further studies into the Boc/solid‐phase synthesis of Ser(P)‐ and Thr(P)‐containing peptides

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri