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Shifting Native Chemical Ligation into Reverse through N→S Acyl Transfer.

Macmillan D, Adams A, Premdjee B - Isr. J. Chem. (2011)

Bottom Line: Reasons for this likely include the often straightforward method of precursor assembly using Fmoc-based chemistry and the fundamentally interesting acyl migration process.In this review we introduce recent advances in this exciting area and discuss, in more detail, our own efforts towards the synthesis of peptide thioesters through N→S acyl transfer in native peptide sequences.We have found that several peptide thioesters can be readily prepared and, what's more, there appears to be ample opportunity for further development and discovery.

View Article: PubMed Central - PubMed

Affiliation: Christopher Ingold Laboratories, Department of Chemistry, University College London 20 Gordon Street, London WC1H 0AJ, UK phone: +44 (0)20 7679 4684 e-mail: d.macmillan@ucl.ac.uk.

ABSTRACT
Peptide thioester synthesis by N→S acyl transfer is being intensively explored by many research groups the world over. Reasons for this likely include the often straightforward method of precursor assembly using Fmoc-based chemistry and the fundamentally interesting acyl migration process. In this review we introduce recent advances in this exciting area and discuss, in more detail, our own efforts towards the synthesis of peptide thioesters through N→S acyl transfer in native peptide sequences. We have found that several peptide thioesters can be readily prepared and, what's more, there appears to be ample opportunity for further development and discovery.

No MeSH data available.


The presence of the carboxyl group appears to accelerate thioester formation, possibly by a) stabilization of the hydroxythiazolidine intermediate, b) increased pKa of the α-amino group (pKa 1> pKa 2) favoring the S-peptide, c) through neighboring group participation.
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sch07: The presence of the carboxyl group appears to accelerate thioester formation, possibly by a) stabilization of the hydroxythiazolidine intermediate, b) increased pKa of the α-amino group (pKa 1> pKa 2) favoring the S-peptide, c) through neighboring group participation.


Shifting Native Chemical Ligation into Reverse through N→S Acyl Transfer.

Macmillan D, Adams A, Premdjee B - Isr. J. Chem. (2011)

The presence of the carboxyl group appears to accelerate thioester formation, possibly by a) stabilization of the hydroxythiazolidine intermediate, b) increased pKa of the α-amino group (pKa 1> pKa 2) favoring the S-peptide, c) through neighboring group participation.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3277902&req=5

sch07: The presence of the carboxyl group appears to accelerate thioester formation, possibly by a) stabilization of the hydroxythiazolidine intermediate, b) increased pKa of the α-amino group (pKa 1> pKa 2) favoring the S-peptide, c) through neighboring group participation.
Bottom Line: Reasons for this likely include the often straightforward method of precursor assembly using Fmoc-based chemistry and the fundamentally interesting acyl migration process.In this review we introduce recent advances in this exciting area and discuss, in more detail, our own efforts towards the synthesis of peptide thioesters through N→S acyl transfer in native peptide sequences.We have found that several peptide thioesters can be readily prepared and, what's more, there appears to be ample opportunity for further development and discovery.

View Article: PubMed Central - PubMed

Affiliation: Christopher Ingold Laboratories, Department of Chemistry, University College London 20 Gordon Street, London WC1H 0AJ, UK phone: +44 (0)20 7679 4684 e-mail: d.macmillan@ucl.ac.uk.

ABSTRACT
Peptide thioester synthesis by N→S acyl transfer is being intensively explored by many research groups the world over. Reasons for this likely include the often straightforward method of precursor assembly using Fmoc-based chemistry and the fundamentally interesting acyl migration process. In this review we introduce recent advances in this exciting area and discuss, in more detail, our own efforts towards the synthesis of peptide thioesters through N→S acyl transfer in native peptide sequences. We have found that several peptide thioesters can be readily prepared and, what's more, there appears to be ample opportunity for further development and discovery.

No MeSH data available.