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Curr Opin Chem Biol. 2014 Oct;22:100-7. doi: 10.1016/j.cbpa.2014.09.024. Epub 2014 Oct 6.

Semi-synthesis of chemokines.

Author information

1
Institute of Biochemistry, Faculty of Bioscience, Pharmacy and Psychology, Leipzig University, Bruederstrasse 34, 04103 Leipzig, Germany. Electronic address: beck-sickinger@uni-leipzig.de.
2
Institute of Biochemistry, Faculty of Bioscience, Pharmacy and Psychology, Leipzig University, Bruederstrasse 34, 04103 Leipzig, Germany.

Abstract

Protein ligation allows the introduction of a wide range of modifications into proteins that are not accessible by mutagenesis. This includes non-proteinogenic amino acids and even backbone modification. This review summarizes recent reports on modified chemokine variants by ligation technologies and includes the development of the first protein with a full secondary structure motif exchanged by a helix that exclusively consists of β-amino acids. Furthermore the first protein activatable by light by rearrangement of a depsi-peptide bond is described. Combining different ligation methods, immobilization and specific release of chemokines were achieved, which is of major importance for the gradient forming activity of chemokines. Examples are shown for CXCL8 (interleukin 8, IL-8) and CXCL12 (stromal derived factor 1, SDF 1) including their chemical and structural characterization as well as the most frequently used assays.

PMID:
25299571
DOI:
10.1016/j.cbpa.2014.09.024
[Indexed for MEDLINE]

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