TY - JOUR
T1 - Fish sarcoplasmic proteins as a high value marine material for wound dressing applications
AU - Vieira, Sara
AU - Franco, Albina R.
AU - Fernandes, Emanuel M.
AU - Amorim, Sara
AU - Ferreira, Helena
AU - Pires, Ricardo A.
AU - Reis, Rui L.
AU - Martins, Albino
AU - Neves, Nuno M.
N1 - Publisher Copyright:
© 2018 Elsevier B.V.
PY - 2018/7/1
Y1 - 2018/7/1
N2 - 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° C, as characterized by differential scanning calorimetry thermograms (DSC). The secondary structure of FSP-E is mainly composed by α-helix structure, as determined by circular dichroism. The cytocompatibility 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 α-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° C, according to the DSC analysis. FSP-M 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.
AB - 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° C, as characterized by differential scanning calorimetry thermograms (DSC). The secondary structure of FSP-E is mainly composed by α-helix structure, as determined by circular dichroism. The cytocompatibility 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 α-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° C, according to the DSC analysis. FSP-M 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.
KW - Cytocompatibility
KW - Membranes
KW - Physico-chemical characterization
KW - Sarcoplasmic proteins
KW - Spin coating
UR - http://www.scopus.com/inward/record.url?scp=85045643360&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2018.04.002
DO - 10.1016/j.colsurfb.2018.04.002
M3 - Article
C2 - 29679807
SN - 0927-7765
VL - 167
SP - 310
EP - 317
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
ER -
