Modern Ligation Methods to Access Natural and Modified Proteins

Authors

  • Alice L. Baumann Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP) Campus Berlin-Buch Robert-Roessle-Str. 10, D-13125 Berlin, Germany; Humboldt-Universität zu Berlin Institut für Chemie Brook-Taylor-Str. 2, D-12489 Berlin, Germany
  • Christian P. R. Hackenberger Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP) Campus Berlin-Buch Robert-Roessle-Str. 10, D-13125 Berlin, Germany; Humboldt-Universität zu Berlin Institut für Chemie Brook-Taylor-Str. 2, D-12489 Berlin. hackenbe@fmp-berlin.de

DOI:

https://doi.org/10.2533/chimia.2018.802

Keywords:

Chemoselective ligation, Native chemical ligation, Protein modification, Protein semi-synthesis

Abstract

Proteins and peptides are gaining increasing interest as tools and targets in fundamental research and drug discovery. Growing research applications have prompted the need for methodologies that produce homogenous peptide and protein material. The development of efficient, chemoselective ligation reactions using unprotected peptide fragments presents a key solution for this challenging task. This review outlines modern ligation methods that enable the synthesis of both native, and also labelled or post-translationally modified peptides and proteins. The ligation methods herein discussed focus on the formation of the backbone amide bond.

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Published

2018-11-30

How to Cite

[1]
A. L. Baumann, C. P. R. Hackenberger, Chimia 2018, 72, 802, DOI: 10.2533/chimia.2018.802.

Issue

Section

Scientific Articles