Abstract
Two oxygen-transporting proteins known for their immunostimulating and anticancer properties, namely hemocyanin from Helix lucorum (HlH) and hemocyanin from Rapana thomasiana (RtH), have been modified for the first time with rosmarinic acid (RA). We prepared two conjugates RA–HlH and RA–RtH containing 47 and 50 rosmarinic acid residues, respectively. The conformational analysis showed that the secondary structure of RA–HlH is less ordered than that of the native HlH, and for the modified protein we observed a decrease in α-helical structures in the favor of random coils, unordered structures, and aggregates. Calorimetric studies showed an increase in the thermal stability of RA–HlH in comparison with the native HlH which is in agreement with the observed structural changes. On the other hand, the conformation of RA–RtH was very similar to that of the native RtH although some rearrangements in the molecule were found. Interestingly, the modification of RtH with RA resulted in a decrease in its thermal stability. A 48-h in vitro experiment showed that tested in concentrations up to 0.7 mg mL−1 the two modified hemocyanins did not inhibit the cell growth of human fibroblasts.
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The financial support of the Bulgarian National Science Fund (Project: ДКOCT 01/27) is gratefully acknowledged.
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Guncheva, M., Todinova, S., Yancheva, D. et al. Rosmarinic acid-conjugated hemocyanins: synthesis and stability. J Therm Anal Calorim 142, 1903–1909 (2020). https://doi.org/10.1007/s10973-020-09738-0
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DOI: https://doi.org/10.1007/s10973-020-09738-0