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The Intrinsic Pepsin Resistance of Interleukin-8 Can be Explained from a Combined Bioinformatical and Experimental Approach

Anders, Gerd and Hassiepen, Ulrich and Theisgen, Stephan and Heymann, Stephan and Muller, Lionel and Panigada, Tania and Huster, Daniel and Samsonov, Sergey (2016) The Intrinsic Pepsin Resistance of Interleukin-8 Can be Explained from a Combined Bioinformatical and Experimental Approach. IEEE TRANSACTIONS ON COMPUTATIONAL BIOLOGY AND BIOINFORMATICS, PP (99). p. 1. ISSN 1545-5963

Abstract

Interleukin-8 (IL-8, CXCL8) is a neutrophil chemotactic factor belonging to the family of chemokines. IL-8 was shown to resist pepsin cleavage displaying its high resistance to this protease. However, the molecular mechanisms underlying this resistance are not fully understood. Using our in-house database containing the data on three-dimensional arrangements of secondary structure elements from the whole Protein Data Bank, we found a striking structural similarity between IL-8 and pepsin inhibitor-3. Such similarity could play a key role in understanding IL-8 resistance to the protease pepsin. To support this hypothesis, we applied pepsin assays confirming that intact IL-8 is not degraded by pepsin in comparison to IL-8 in a denaturated state. Applying 1H-15N Heteronuclear Single Quantum Coherence NMR measurements, we determined the putative regions at IL-8 that are potentially responsible for interactions with the pepsin. The results obtained in this work contribute to the understanding of the resistance of IL-8 to pepsin proteolysis in terms of its structural properties.

Item Type: Article
Keywords: Immune system, Proteins, Databases, Electronic mail, Three-dimensional displays, Fluorescence, Bioinformatics, interleukin-8, Protein-protein interactions, computational biology, pepsin resistance, pepsin inhibitor
Date Deposited: 09 Nov 2016 00:45
Last Modified: 09 Nov 2016 00:45
URI: https://oak.novartis.com/id/eprint/29106

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