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Artificial Chemokines: Combining Chemistry and Molecular Biology for the Elucidation of Interleukin-8 Functionality

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Institut für Biochemie, Fakultät für Biowissenschaften, Pharmazie and Psychologie, Universität Leipzig, Brüderstrasse 34, D-04103 Leipzig, Germany, and Laboratorium für Organische Chemie, ETH Zürich, Hönggerberg HCI, CH-8093 Zürich, Switzerland
[email protected]
†Universität Leipzig.
‡ETH Zürich, Hönggerberg HCI.
Cite this: J. Am. Chem. Soc. 2008, 130, 46, 15311–15317
Publication Date (Web):October 22, 2008
https://doi.org/10.1021/ja802453x
Copyright © 2008 American Chemical Society
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    Abstract

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    How can we understand the contribution of individual parts or segments to complex structures? A typical strategy to answer this question is simulation of a segmental replacement followed by realization and investigation of the resulting effect in structure−activity studies. For proteins, this problem is commonly addressed by site-directed mutagenesis. A more general approach represents the exchange of whole secondary structure elements by rationally designed segments. For a demonstration of this possibility we identified the α-helix at the C-terminus of human interleukin-8 (hIL-8). Since this chemokine possesses four conserved cysteine residues, it can easily be altered by ligation strategies. A set of different segments, which are able to form amphiphilic helices, was synthesized to mimic the C-terminal α-helix. Beside sequences of α-amino acids, oligomers of non-natural β3-amino acids with the side chains of canonical amino acids were introduced. Such β-peptides form helices, which differ from the α-helix in handedness and dipole orientation. Variants of the semisynthetic hIL-8 proteins demonstrated clearly that the exact side chain orientation is of more importance than helix handedness and dipole orientation. The activity of a chimeric protein with a β-peptide helix that mimics the side chain orientation of the native α-helix most perfectly is comparable to that of the native hIL-8. Concepts like this could be a first step toward the synthesis of proteins consisting of large artificial secondary structure elements.

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    Supporting Information includes a detailed description on cloning of hIL-8 cDNA, purification of hIL-8 (1−77), and CD, HPLC, and FT-ICR mass spectra of the various hIL8-analogues. This material is available free of charge via the Internet at http://pubs.acs.org.

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