1,520
Views
0
CrossRef citations to date
0
Altmetric
Article

Biophysical characterization of the structural stability of Helix lucorum hemocyanin

, , , , &
Pages 18-28 | Received 11 Jun 2020, Accepted 09 Oct 2020, Published online: 03 Nov 2020

References

  • Préaux G, Gielens C. Hemocyanins. In: Lontie R, editor. Copper proteins and copper enzymes. Vol. 2. Boca Raton, FL: CRC Press; 1984. p. 159–205.
  • van Holde KE, Miller KI. Hemocyanins. Adv Protein Chem. 1995;47:1–81.
  • Gesheva V, Chausheva S, Stefanova N, et al. Helix Pomatia hemocyanin - a novel bio-adjuvant for viral and bacterial antigens. Int Immunopharmacol. 2015;26(1):162–168.
  • Gesheva V, Chausheva S, Mihaylova N, et al. Anti-cancer properties of gastropodan hemocyanins in murine model of colon carcinoma. BMC Immunol. 2014;15:34–44.
  • Zanjani NT, Saksena MM, Dehghani F, et al. From ocean to bedside: the therapeutic potential of molluscan hemocyanins. Curr Med Chem. 2018;25(20):2292–2303.
  • Stoyanova E, Mihaylova N, Manoylov I, et al. Intensive therapy with gastropodan hemocyanins increases their antitumor properties in murine model of colon carcinoma. Int Immunopharmacol. 2020;84:106566.
  • Dolashka-Angelova P, Stefanova T, Livaniou E, et al. Immunological potential of Helix vulgaris and Rapana venosa hemocyanins. Immunol Invest. 2008;37(8):822–840.
  • Dolashka P, Velkova L, Iliev I, et al. Antitumor activity of glycosylated molluscan hemocyanins via Guerin ascites tumor. Immunol Invest. 2011;40(2):130–149.
  • Boyanova O, Dolashka P, Toncheva D, et al. In vitro effect of molluscan hemocyanins on CAL-29 and T-24 bladder cancer cell lines. Biomed Rep. 2013;1(2):235–238.
  • Kelly SM, Jess TJ, Price NC. How to study proteins by circular dichroism. Biochim Biophys Acta. 2005;1751(2):119–139.
  • Remmele RL. Microcalorimetric approaches to biopharmaceutical development. In: Rodriguez-Diaz R, Wehr T, Tuck S, editors, Analytical techniques for biopharmaceutical development. New York, USA: Taylor & Francis; 2005. p. 327–381.
  • Demarest SJ, Frasca V. Differential scanning calorimetry in the biopharmaceutical sciences. In: Houde DJ, Berkowitz SA, editors, Biophysical characterization of proteins in developing biopharmaceuticals. Amsterdam, Netherlands: Elsevier; 2015. p. 287–306.
  • Idakieva K, Parvanova K, Todinova S. Differential scanning calorimetry of the irreversible denaturation of Rapana thomasiana (marine snail, Gastropod) hemocyanin. Biochim Biophys Acta. 2005;1748(1):50–56.
  • Idakieva K, Gielens C, Siddiqui NI, et al. Irreversible thermal denaturation of β-hemocyanin of Helix pomatia and its substructures studied by differential scanning calorimetry. Z Naturforschung A. 2007;62(9):499–506.
  • Idakieva K, Nikolov P, Chakarska I, et al. Spectroscopic properties and conformational stability of Concholepas concholepas hemocyanin. J Fluoresc. 2008;18(3–4):715–725.
  • Idakieva K, Meersman F, Gielens C. Reversible heat inactivation of copper sites precedes thermal unfolding of molluscan (Rapana thomasiana) hemocyanin. Biochim Biophys Acta. 2012;1824(5):731–738.
  • Todinova S, Raynova Y, Idakieva K. Irreversible thermal denaturation of Helix aspersa maxima hemocyanin. J Therm Anal Calorim. 2018;132(1):777–786.
  • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248–254.
  • Dolashki A, Velkova L, Voelter W, et al. Structural and conformational stability of hemocyanin from the garden snail Cornu aspersum. Z Naturforsch C J Biosci. 2019; 74(5–6):113–123.
  • Gielens C, De Sadeleer J, Preaux G, et al. Identification, separation and cheracterization of the hemocyanin components of Helix aspersa. Comp Biochem Physiol. 1987;88(1):181–186.
  • Lumry R, Eyring H. Conformation changes of proteins. J Phys Chem. 1954;58(2):110–120.
  • Kurganov BI, Lyubarev AE, Sanchez-Ruiz JM, et al. Analysis of differential scanning calorimetry data for proteins, criteria of validity of one-step mechanism of irreversible protein denaturation. Biophys Chem. 1997;69(2–3):125–135.
  • Meissner U, Gatsogiannis C, Moeller A, et al. Comparative 11A structure of two molluscan hemocyanins from 3D cryo-electron microscopy. Micron. 2007;38(7):754–765.
  • Markl J. Evolution of molluscan hemocyanin structures. Biochim Biophys Acta. 2013;1834(9):1840–1852.
  • Idakieva K, Schwarz H, Genov N, et al. Rapana thomasiana hemocyanin (RtH): dissociation and reassociation behavior of two isoforms, RtH1 and RtH2. Micron. 2002;33(1):7–14.
  • Velkova L, Dimitrov I, Schwarz H, et al. Structure of hemocyanin from garden snail Helix lucorum. Comp Biochem Physiol B Biochem Mol Biol. 2010;157(1):16–25.
  • Varshney A, Ahmad B, Rabbani G, et al. Acid-induced unfolding of didecameric keyhole limpet hemocyanin: detection and characterizations of decameric and tetrameric intermediate states. Amino Acids. 2010;39(3):899–910.
  • Georgieva DN, Stoeva S, Ali SA, et al. Circular dichroism study of the hemocyanin thermostability. Spectrochim Acta A. 1998;54(5):765–771.
  • Dolashki A, Schutz J, Hristova R, et al. Spectroscopic properties of non-glycosilated functional unit KLH2-c of keyhole limpet hemocyanin. World J Agric Sci. 2005; 1:129–136.
  • Dolashki A, Velkova L, Atanasov B, et al. Reversibility and “"pH-T phase diagrams" of Rapana venosa hemocyanin and its structural subunits”. Biochim Biophys Acta. 2008;1784(11):1617–1624.
  • Marshall G, Valtchev P, Dehghani F, et al. Thermal denaturation and protein stability analysis of Haliotis rubra hemocyanin. J Therm Anal Calorim. 2016;123(3):2499–2505.
  • Guzman-Casado M, Parody-Morreale A, Mateo PL, et al. Differential scanning calorimetry of lobster haemocyanin. Eur J Biochem. 1990;188(1):181–185.
  • Sanchez-Ruiz JM. Protein kinetic stability. Biophys Chem. 2010;148(1-3):1–15.
  • Shnyrov V, Zhadan G, Akoev I. Calorimetric measurements of the effect of 330-MHz radiofrequency radiation on human erythrocyte ghosts. Bioelectromagnetics. 1984;5(4):411–418.
  • Shnyrov V, Mateo P. Thermal transitions in the purple membrane from Halobacterium halobium. FEBS Lett. 1993;324(2):237–240.
  • Lyubarev AE, Kurganov BI. Analysis of DSC data relating to proteins undergoing irreversible thermal denaturation. J Therm Anal Calorim. 2000;62(1):51–62.
  • Wood EJ, Chaplin MF, Gielens C, et al. Relative molecular mass of the polypeptide chain of β-haemocyanin of Helix pomatia and carbohydrate composition of the functional units. Comp Biochem Physiol. 1985;82(1):179–186.
  • Idakieva K, Stoeva S, Voelter W, et al. Glycosylation of Rapana thomasiana Hemocyanin. Comparison with other prosobranch (Gastropod) hemocyanins. Comp Biochem Physiol B Biochem Mol Biol. 2004;138(3):221–228.