Fish sarcoplasmic proteins as a high value marine material for wound dressing applications

Fish sarcoplasmic proteins (FSP) constitute around 25-30% of the total fish muscle protein. As the FSP are water soluble, FSP were isolated from fresh cod (Gadus morhua) by centrifugation. By SDS-PAGE, it was possible to determine the composition of FSP extracts (FSP-E). The FSP-E undergo denaturation at 44.12 +/- 2.34 degrees C, as characterized by differential scanning calorimetry thermograms (DSC). The secondary structure of FSP-E is mainly composed by alpha-helix structure, as determined by circular dichroism. The cyto-compatibility of FSP-E, at concentrations ranging from 5 to 20 mg/mL, was investigated. Concentrations lower than 10 mg/mL have no cytotoxicity cultures of fibroblasts over 72 h. Further on, FSP membranes (FSP-M) were produced by spin coating to evaluate its properties. FSP-M shown having uniform surface as analyzed by Scanning Electron Microscopy (SEM). The relative amount of alpha-helix structures is higher when compared with the FSP-E. The FSP-M have higher temperature stability than the FSP-E, since they presented a denaturation temperature of 58.88 +/- 3.36 degrees C, according to the DSC analysis. FSPM shown distinctive mechanical properties, with a stiffness of 16.57 +/- 3.95 MPa and a yield strength of 23.85 +/- 5.97 MPa. Human lung fibroblasts cell lines (MRC-5) were cultured in direct contact with FSP-M, demonstrating its cytocompatibility for 48 h. Based on these results, FSP can be considered a potential biomaterial recovered from nature, for wound dressing applications. (C) 2018 Elsevier B.V. All rights reserved.