Inhibition of Collagenase by Mycosporine-like Amino Acids from Marine Sources

Anja Hartmann; Johanna Gostner; Julian E. Fuchs; Eliza Chaita; Nektarios Aligiannis; Leandros Skaltsounis; Markus Ganzera

doi:10.1055/s-0035-1546105

Planta Medica, Table of Contents

Planta Med 2015; 81(10): 813-820
DOI: 10.1055/s-0035-1546105

Biological and Pharmacological Activity

Original Papers

Georg Thieme Verlag KG Stuttgart · New York

Inhibition of Collagenase by Mycosporine-like Amino Acids from Marine Sources

Anja Hartmann

¹Institute of Pharmacy, Pharmacognosy, University of Innsbruck, Innsbruck, Austria

,

Johanna Gostner

²Medical Biochemistry, Biocenter, Medical University of Innsbruck, Innsbruck, Austria

,

Julian E. Fuchs

³Center for Molecular Informatics, Department of Chemistry, University of Cambridge, Cambridge, United Kingdom

,

Eliza Chaita

⁴Department of Pharmacognosy and Natural Products Chemistry, Faculty of Pharmacy, University of Athens, Athens, Greece

,

Nektarios Aligiannis

⁴Department of Pharmacognosy and Natural Products Chemistry, Faculty of Pharmacy, University of Athens, Athens, Greece

,

Leandros Skaltsounis

⁴Department of Pharmacognosy and Natural Products Chemistry, Faculty of Pharmacy, University of Athens, Athens, Greece

,

Markus Ganzera

¹Institute of Pharmacy, Pharmacognosy, University of Innsbruck, Innsbruck, Austria

› Author Affiliations

Abstract

Matrix metalloproteinases play an important role in extracellular matrix remodeling. Excessive activity of these enzymes can be induced by UV light and leads to skin damage, a process known as photoaging. In this study, we investigated the collagenase inhibition potential of mycosporine-like amino acids, compounds that have been isolated from marine organisms and are known photoprotectants against UV-A and UV-B. For this purpose, the commonly used collagenase assay was optimized and for the first time validated in terms of relationships between enzyme-substrate concentrations, temperature, incubation time, and enzyme stability. Three compounds were isolated from the marine red algae Porphyra sp. and Palmaria palmata, and evaluated for their inhibitory properties against Chlostridium histolyticum collagenase. A dose-dependent, but very moderate, inhibition was observed for all substances and IC₅₀ values of 104.0 µM for shinorine, 105.9 µM for porphyra, and 158.9 µM for palythine were determined. Additionally, computer-aided docking models suggested that the mycosporine-like amino acids binding to the active site of the enzyme is a competitive inhibition.

Key words

collagenase - mycosporine-like amino acids - algae - skin aging

Full Text

References

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