Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation. / Chisholm, Timothy S.; Kulkarni, Sameer S.; Hossain, Khondker R.; Cornelius, Flemming; Clarke, Ronald J.; Payne, Richard J.

I: Journal of the American Chemical Society, Bind 142, Nr. 2, 2020, s. 1090-1100.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Chisholm, TS, Kulkarni, SS, Hossain, KR, Cornelius, F, Clarke, RJ & Payne, RJ 2020, 'Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation', Journal of the American Chemical Society, bind 142, nr. 2, s. 1090-1100. https://doi.org/10.1021/jacs.9b12558

APA

Chisholm, T. S., Kulkarni, S. S., Hossain, K. R., Cornelius, F., Clarke, R. J., & Payne, R. J. (2020). Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation. Journal of the American Chemical Society, 142(2), 1090-1100. https://doi.org/10.1021/jacs.9b12558

CBE

Chisholm TS, Kulkarni SS, Hossain KR, Cornelius F, Clarke RJ, Payne RJ. 2020. Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation. Journal of the American Chemical Society. 142(2):1090-1100. https://doi.org/10.1021/jacs.9b12558

MLA

Chisholm, Timothy S. o.a.. "Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation". Journal of the American Chemical Society. 2020, 142(2). 1090-1100. https://doi.org/10.1021/jacs.9b12558

Vancouver

Chisholm TS, Kulkarni SS, Hossain KR, Cornelius F, Clarke RJ, Payne RJ. Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation. Journal of the American Chemical Society. 2020;142(2):1090-1100. https://doi.org/10.1021/jacs.9b12558

Author

Chisholm, Timothy S. ; Kulkarni, Sameer S. ; Hossain, Khondker R. ; Cornelius, Flemming ; Clarke, Ronald J. ; Payne, Richard J. / Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation. I: Journal of the American Chemical Society. 2020 ; Bind 142, Nr. 2. s. 1090-1100.

Bibtex

@article{dd4c8f693ad44c5e9b5706bfdc437235,
title = "Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation",
abstract = "Peptide ligation chemistry has revolutionized protein science by providing access to homogeneously modified peptides and proteins. However, lipidated polypeptides and integral membrane proteins - an important class of biomolecules - remain enormously challenging to access synthetically owing to poor aqueous solubility of one or more of the fragments under typical ligation conditions. Herein we describe the advent of a reductive diselenide-selenoester ligation (rDSL) method that enables efficient ligation of peptide fragments down to low nanomolar concentrations, without resorting to solubility tags or hybridizing templates. The power of rDSL is highlighted in the efficient synthesis of the FDA-approved therapeutic lipopeptide tesamorelin and palmitylated variants of the transmembrane lipoprotein phospholemman (FXYD1). Lipidation of FXYD1 was shown to critically modulate inhibitory activity against the Na+/K+ pump.",
author = "Chisholm, {Timothy S.} and Kulkarni, {Sameer S.} and Hossain, {Khondker R.} and Flemming Cornelius and Clarke, {Ronald J.} and Payne, {Richard J.}",
year = "2020",
doi = "10.1021/jacs.9b12558",
language = "English",
volume = "142",
pages = "1090--1100",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "2",

}

RIS

TY - JOUR

T1 - Peptide Ligation at High Dilution via Reductive Diselenide-Selenoester Ligation

AU - Chisholm, Timothy S.

AU - Kulkarni, Sameer S.

AU - Hossain, Khondker R.

AU - Cornelius, Flemming

AU - Clarke, Ronald J.

AU - Payne, Richard J.

PY - 2020

Y1 - 2020

N2 - Peptide ligation chemistry has revolutionized protein science by providing access to homogeneously modified peptides and proteins. However, lipidated polypeptides and integral membrane proteins - an important class of biomolecules - remain enormously challenging to access synthetically owing to poor aqueous solubility of one or more of the fragments under typical ligation conditions. Herein we describe the advent of a reductive diselenide-selenoester ligation (rDSL) method that enables efficient ligation of peptide fragments down to low nanomolar concentrations, without resorting to solubility tags or hybridizing templates. The power of rDSL is highlighted in the efficient synthesis of the FDA-approved therapeutic lipopeptide tesamorelin and palmitylated variants of the transmembrane lipoprotein phospholemman (FXYD1). Lipidation of FXYD1 was shown to critically modulate inhibitory activity against the Na+/K+ pump.

AB - Peptide ligation chemistry has revolutionized protein science by providing access to homogeneously modified peptides and proteins. However, lipidated polypeptides and integral membrane proteins - an important class of biomolecules - remain enormously challenging to access synthetically owing to poor aqueous solubility of one or more of the fragments under typical ligation conditions. Herein we describe the advent of a reductive diselenide-selenoester ligation (rDSL) method that enables efficient ligation of peptide fragments down to low nanomolar concentrations, without resorting to solubility tags or hybridizing templates. The power of rDSL is highlighted in the efficient synthesis of the FDA-approved therapeutic lipopeptide tesamorelin and palmitylated variants of the transmembrane lipoprotein phospholemman (FXYD1). Lipidation of FXYD1 was shown to critically modulate inhibitory activity against the Na+/K+ pump.

UR - http://www.scopus.com/inward/record.url?scp=85077936625&partnerID=8YFLogxK

U2 - 10.1021/jacs.9b12558

DO - 10.1021/jacs.9b12558

M3 - Journal article

C2 - 31840988

AN - SCOPUS:85077936625

VL - 142

SP - 1090

EP - 1100

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 2

ER -