One-Pot Peptide Ligation–Desulfurization at Glutamate

Katie M. Cergol; Robert E. Thompson; Lara R. Malins; Peter Turner; Richard J. Payne

doi:10.1021/ol403288n

One-Pot Peptide Ligation–Desulfurization at Glutamate

Katie M. Cergol, Robert E. Thompson, Lara R. Malins, Peter Turner, Richard J. Payne^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

73 Citations (SciVal)

Abstract

An efficient methodology for ligation at glutamate (Glu) is described. A γ-thiol-Glu building block was accessed in only three steps from protected glutamic acid and could be incorporated at the N-terminus of peptides. The application of these peptides in one-pot ligation-desulfurization chemistry is demonstrated with a range of peptide thioesters, and the utility of this methodology is highlighted through the synthesis of the osteoporosis peptide drug teriparatide (Forteo).

Original language	English
Pages (from-to)	290-293
Number of pages	4
Journal	Organic Letters
Volume	16
Issue number	1
Early online date	2 Dec 2013
DOIs	https://doi.org/10.1021/ol403288n
Publication status	Published - 3 Jan 2014
Externally published	Yes

Access to Document

10.1021/ol403288n

Cite this

@article{6706a2fe5615494abff31502a6b0f14e,

title = "One-Pot Peptide Ligation–Desulfurization at Glutamate",

abstract = "An efficient methodology for ligation at glutamate (Glu) is described. A γ-thiol-Glu building block was accessed in only three steps from protected glutamic acid and could be incorporated at the N-terminus of peptides. The application of these peptides in one-pot ligation-desulfurization chemistry is demonstrated with a range of peptide thioesters, and the utility of this methodology is highlighted through the synthesis of the osteoporosis peptide drug teriparatide (Forteo).",

author = "Cergol, \{Katie M.\} and Thompson, \{Robert E.\} and Malins, \{Lara R.\} and Peter Turner and Payne, \{Richard J.\}",

year = "2014",

month = jan,

day = "3",

doi = "10.1021/ol403288n",

language = "English",

volume = "16",

pages = "290--293",

journal = "Organic Letters",

issn = "1523-7060",

publisher = "American Chemical Society",

number = "1",

}

TY - JOUR

T1 - One-Pot Peptide Ligation–Desulfurization at Glutamate

AU - Cergol, Katie M.

AU - Thompson, Robert E.

AU - Malins, Lara R.

AU - Turner, Peter

AU - Payne, Richard J.

PY - 2014/1/3

Y1 - 2014/1/3

N2 - An efficient methodology for ligation at glutamate (Glu) is described. A γ-thiol-Glu building block was accessed in only three steps from protected glutamic acid and could be incorporated at the N-terminus of peptides. The application of these peptides in one-pot ligation-desulfurization chemistry is demonstrated with a range of peptide thioesters, and the utility of this methodology is highlighted through the synthesis of the osteoporosis peptide drug teriparatide (Forteo).

AB - An efficient methodology for ligation at glutamate (Glu) is described. A γ-thiol-Glu building block was accessed in only three steps from protected glutamic acid and could be incorporated at the N-terminus of peptides. The application of these peptides in one-pot ligation-desulfurization chemistry is demonstrated with a range of peptide thioesters, and the utility of this methodology is highlighted through the synthesis of the osteoporosis peptide drug teriparatide (Forteo).

UR - https://www.scopus.com/pages/publications/84891807632

U2 - 10.1021/ol403288n

DO - 10.1021/ol403288n

M3 - Article

SN - 1523-7060

VL - 16

SP - 290

EP - 293

JO - Organic Letters

JF - Organic Letters

IS - 1

ER -

One-Pot Peptide Ligation–Desulfurization at Glutamate

Abstract

Access to Document

Other files and links

Fingerprint

Cite this