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Molecules 2015, 20(9), 15449-15468; doi:10.3390/molecules200915449

Autodisplay of Human Hyaluronidase Hyal-1 on Escherichia coli and Identification of Plant-Derived Enzyme Inhibitors

1
Institute of Pharmaceutical and Medicinal Chemistry, Phytochemistry, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstr. 48, 48149 Münster, Germany
2
Institute of Pharmacy, Pharmaceutical Biology, Freie Universität Berlin, Königin-Luise Str. 2+4, 14195 Berlin, Germany
3
Department of Pharmaceutical/Medicinal Chemistry II, Institute of Pharmacy, University Regensburg, Universitätsstr. 31, 93040 Regensburg, Germany
4
Institute of Pharmaceutical Biology and Phytochemistry, PharmaCampus, Westfälische Wilhelms-Universität Münster, Corrensstr. 48, 48149 Münster, Germany
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Thomas J. Schmidt
Received: 2 July 2015 / Revised: 17 August 2015 / Accepted: 18 August 2015 / Published: 26 August 2015
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Abstract

Hyaluronan (HA) is the main component of the extracellular matrix (ECM). Depending on its chain size, it is generally accepted to exert diverse effects. High molecular weight HA is anti-angiogenic, immunosuppressive and anti-inflammatory, while lower fragments are angiogenic and inflammatory. Human hyaluronidase Hyal-1 (Hyal-1) is one of the main enzymes in the metabolism of HA. This makes Hyal-1 an interesting target. Not only for functional and mechanistic studies, but also for drug development. In this work, Hyal-1 was expressed on the surface of E. coli, by applying Autodisplay, to overcome formation of inactive “inclusion bodies”. With the cells displaying Hyal-1 an activity assay was performed using “stains-all” dye. Subsequently, the inhibitory effects of four saponins and 14 plant extracts on the activity of surface displayed Hyal-1 were evaluated. The determined IC50 values were 177 µM for glycyrrhizic acid, 108 µM for gypsophila saponin 2, 371 µM for SA1657 and 296 µM for SA1641. Malvae sylvestris flos, Equiseti herba and Ononidis radix extracts showed IC50 values between 1.4 and 1.7 mg/mL. In summary, Autodisplay enabled the expression of functional human target protein Hyal-1 in E. coli and facilitated an accelerated testing of potential inhibitors. View Full-Text
Keywords: Autodisplay; Hyal-1; hyaluronan; natural inhibitors Autodisplay; Hyal-1; hyaluronan; natural inhibitors
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Orlando, Z.; Lengers, I.; Melzig, M.F.; Buschauer, A.; Hensel, A.; Jose, J. Autodisplay of Human Hyaluronidase Hyal-1 on Escherichia coli and Identification of Plant-Derived Enzyme Inhibitors. Molecules 2015, 20, 15449-15468.

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