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Selenopeptide transamidation and metathesis.

Ollivier N, Blanpain A, Boll E, Raibaut L, Drobecq H, Melnyk O - Org. Lett. (2014)

Bottom Line: Selenopeptides can be transamidated by cysteinyl peptides in water using mild conditions (pH 5.5, 37 °C) in the presence of an arylthiol catalyst.Similar conditions also catalyze the metathesis of selenopeptides.The usefulness of the selenophosphine derived from TCEP (TCEP═Se) for inhibiting the TCEP-induced deselenization of selenocysteine residue is also reported.

View Article: PubMed Central - PubMed

Affiliation: CNRS UMR 8161, Institut Pasteur de Lille, Université Lille Nord de France , 59021 Lille, France.

ABSTRACT
Selenopeptides can be transamidated by cysteinyl peptides in water using mild conditions (pH 5.5, 37 °C) in the presence of an arylthiol catalyst. Similar conditions also catalyze the metathesis of selenopeptides. The usefulness of the selenophosphine derived from TCEP (TCEP═Se) for inhibiting the TCEP-induced deselenization of selenocysteine residue is also reported.

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Kinetic rates of the selenopeptide metathesis reactions and HPLCprofiles of the crude metathesis reactions.
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fig1: Kinetic rates of the selenopeptide metathesis reactions and HPLCprofiles of the crude metathesis reactions.

Mentions: We next examined the possibility to perform a metathesis reactionusing selenopeptides 5e (X = Ala) and 3d (X = Arg) and MPAA as catalyst (Scheme 5).Hopefully, the reaction showed the formation of two novel selenopeptideproducts, peptides 5d and 3e (Figure 1a), which coeluted with authentic samples by HPLC.The identity of these compounds was further confirmed by extensivemass spectrometry fragmentation analysis. We observed also two otherproducts, i.e., peptides ILKEPVHGA-OH and ILKEPVHGR-OH, arising fromthe X-Sec peptide bond hydrolysis (peptides 8d,e, Figure 1a). The level of hydrolysis products 8d and 8e remained below 10% after 100 h (see FiguresS24 and S27 in the Supporting Information).


Selenopeptide transamidation and metathesis.

Ollivier N, Blanpain A, Boll E, Raibaut L, Drobecq H, Melnyk O - Org. Lett. (2014)

Kinetic rates of the selenopeptide metathesis reactions and HPLCprofiles of the crude metathesis reactions.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4120982&req=5

fig1: Kinetic rates of the selenopeptide metathesis reactions and HPLCprofiles of the crude metathesis reactions.
Mentions: We next examined the possibility to perform a metathesis reactionusing selenopeptides 5e (X = Ala) and 3d (X = Arg) and MPAA as catalyst (Scheme 5).Hopefully, the reaction showed the formation of two novel selenopeptideproducts, peptides 5d and 3e (Figure 1a), which coeluted with authentic samples by HPLC.The identity of these compounds was further confirmed by extensivemass spectrometry fragmentation analysis. We observed also two otherproducts, i.e., peptides ILKEPVHGA-OH and ILKEPVHGR-OH, arising fromthe X-Sec peptide bond hydrolysis (peptides 8d,e, Figure 1a). The level of hydrolysis products 8d and 8e remained below 10% after 100 h (see FiguresS24 and S27 in the Supporting Information).

Bottom Line: Selenopeptides can be transamidated by cysteinyl peptides in water using mild conditions (pH 5.5, 37 °C) in the presence of an arylthiol catalyst.Similar conditions also catalyze the metathesis of selenopeptides.The usefulness of the selenophosphine derived from TCEP (TCEP═Se) for inhibiting the TCEP-induced deselenization of selenocysteine residue is also reported.

View Article: PubMed Central - PubMed

Affiliation: CNRS UMR 8161, Institut Pasteur de Lille, Université Lille Nord de France , 59021 Lille, France.

ABSTRACT
Selenopeptides can be transamidated by cysteinyl peptides in water using mild conditions (pH 5.5, 37 °C) in the presence of an arylthiol catalyst. Similar conditions also catalyze the metathesis of selenopeptides. The usefulness of the selenophosphine derived from TCEP (TCEP═Se) for inhibiting the TCEP-induced deselenization of selenocysteine residue is also reported.

Show MeSH
Related in: MedlinePlus