Biophysical properties and cytotoxicity of feruloylated helix lucorum hemocyanin

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creativework.keywordsConformational stability, Cytotoxicity, Ferulic acid, Hemocyanin conjugates, Thermal stability
creativework.publisherSlovensko Kemijsko Drustvoen
dc.contributor.authorGuncheva M.
dc.contributor.authorIdakieva K.
dc.contributor.authorTodinova S.
dc.contributor.authorStoyanova E.
dc.contributor.authorYancheva D.
dc.date.accessioned2024-07-10T14:27:04Z
dc.date.accessioned2024-07-10T14:49:32Z
dc.date.available2024-07-10T14:27:04Z
dc.date.available2024-07-10T14:49:32Z
dc.date.issued2020-03-20
dc.description.abstractFor 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.
dc.identifier.doi10.17344/acsi.2019.5400
dc.identifier.issn1580-3155
dc.identifier.issn1318-0207
dc.identifier.scopusSCOPUS_ID:85082313080en
dc.identifier.urihttps://rlib.uctm.edu/handle/123456789/580
dc.language.isoen
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85082313080&origin=inward
dc.titleBiophysical properties and cytotoxicity of feruloylated helix lucorum hemocyanin
dc.typeArticle
oaire.citation.issue1
oaire.citation.volume67
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