Abstract

Recently, the bioactive properties of marine collagen and marine collagen hydrolysates have been demonstrated. Although there is some literature assessing the general chemical features and biocompatibility of collagen extracts from marine sponges, no data are available on the biological effects of sponge collagen hydrolysates for biomedical and/or cosmetic purposes. Here, we studied the in vitro toxicity, antioxidant, wound-healing, and photoprotective properties of four HPLC-purified fractions of trypsin-digested collagen extracts—marine collagen hydrolysates (MCHs)—from the marine sponge C. reniformis. The results showed that the four MCHs have no degree of toxicity on the cell lines analyzed; conversely, they were able to stimulate cell growth. They showed a significant antioxidant activity both in cell-free assays as well as in H2O2 or quartz-stimulated macrophages, going from 23% to 60% of reactive oxygen species (ROS) scavenging activity for the four MCHs. Finally, an in vitro wound-healing test was performed with fibroblasts and keratinocytes, and the survival of both cells was evaluated after UV radiation. In both experiments, MCHs showed significant results, increasing the proliferation speed and protecting from UV-induced cell death. Overall, these data open the way to the use of C. reniformis MCHs in drug and cosmetic formulations for damaged or photoaged skin repair.

Highlights

  • Collagens constitute a variegated family of structural proteins that are usually found in the extracellular matrix (ECM) of many tissues in multicellular organisms

  • We undertook our study by choosing a marine sponge that was enriched in collagen, whose chemical and bioactive properties have already been in part documented as in the case of C. reniformis

  • The collagen of this demosponge already holds promising features for its use in the production of biomaterials that are suitable for tissue engineering and regenerative medicine purposes, as has been recently demonstrated by our group

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Summary

Introduction

Collagens constitute a variegated family of structural proteins that are usually found in the extracellular matrix (ECM) of many tissues in multicellular organisms. They participate in the formation of a complex glycosaminoglycan/protein network ensuing the structural support and physiological integrity of the tissues, mainly, but not exclusively, of mesodermal origin. Thanks to their low immunogenicity across the species and the remarkable mechanical and/or bioactive properties, Mar. Drugs 2018, 16, 465; doi:10.3390/md16120465 www.mdpi.com/journal/marinedrugs. Drugs 2018, 16, 465 their collagen extracts, derived gelatins, and peptide hydrolysates are frequently used in health-related sectors [1], cosmetics, and the food industry [2].

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