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Biophysical Properties and Cytotoxicity of Feruloylated Helix Lucorum Hemocyanin

Maya Guncheva, Krassimira Idakieva, Svetla Todinova, Elena Stoyanova, Denitsa Yancheva

Abstract


For the first time Helix lucorum hemocyanin (HlH) has been feruloylated. Two HlH conjugates with 40- and 120- ferulic acid residues were prepared, denoted as FA-HlH-1 and FA-HlH-2. Expectedly, the feruloylation of HlH induced a rearrangement of the protein molecule, a decrease in the α-helical structure at the expense of β-structures was observed. Besides, the FA-HlH conjugates were more prone to aggregation, which is probably due to the stabilization of the partially unfolded protein molecules by non-covalent bonding. Interestingly, the thermal stability of HlH was not affected by the modification. The native and feruloylated HlH were not toxic to normal fibroblasts (BJ cells). We observed a decrease in cell viability of breast cancer MCF-7 cells to about 66% after a 48h exposure to 70 µg/well of FA-HlH-2.


Keywords


Hemocyanin conjugates; ferulic acid; conformational stability; thermal stability; cytotoxicity

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DOI: http://dx.doi.org/10.17344/acsi.2019.5400

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Copyright (c) 2019 Maya Guncheva, Krassimira Idakieva, Svetla Todinova, Elena Stoyanova, Denitsa Yancheva

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