Bence-Jones protein as the form of nano-scaled β-stacked supramolecular aggregates

  • N. M. Voroshylova State Institution «O.C. Kolomiychenko Institute of Otolaryngology of the National Academy of Medical Sciences of Ukraine»
  • M. D. Timchenko State Institution «O.C. Kolomiychenko Institute of Otolaryngology of the National Academy of Medical Sciences of Ukraine»
  • S. V. Verevka State Institution «O.C. Kolomiychenko Institute of Otolaryngology of the National Academy of Medical Sciences of Ukraine»
Keywords: protein aggregation, amyloidoses, β-aggregates, congophilia, Bence-Jones protein.


Abstract. The formation in β-structured protein aggregates in tissues and fluids of the body is one of the most dangerouse complications of various diseases. The most famous of them are amyloidoses, but they such deposits are observed at other, much more widespread, diseases. The generally accepted approach to amyloids’detectionis based on  high-specific coloring by Congo Red dye. However, the Abbe's diffraction limit excludes the seeing of the objects smaller than 0.61 wavelengths (about 240 nm). Such nanoscale formations are capable to disrup the functioning of surrounding tissues, to causethe complications and recurrences of the disease, and to pass through biological barriers with the following accumulation in body’s fluids. It’s likely that these conditions are the cause of the urinary congophilia, that is associated with preeclampsia at pregnancy and chronic kidney disease. Nor the less suspicious object is the Bens-Jones protein that appears in the urine at multiple myeloma and some other diseases, which are in more or less extent,are related to the disturbance of protein metabolism.

The purpose of this study was to clarify the aggregate state of the Bens-Jones protein as a possible β-structured supramolecular associate.

Methods.The subject of the study was the freshly received urine from a patient with multiple myeloma. The presence of the Bens-Jones protein was checked by thermopacification of the acidified sample. For control, the urine was used by a healthy person with the addition of certain amounts of human serum albumin ("Reanal", Hungary) with a concentration of 0, 0.01, 0.1 and 1%.

Result. The obtained data testify to the appropriateness of such a point of view and create preresquites for the expanding of diagnostic possibilities.

Conclusions.The results obtained during the study testify to the peculiarity of the structure of the Bens-Jones protein, which is nano-sized beta-structured supramolecular


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Pupkova VI, Prasolova L. Opredelenie belka v moche i spinnomozgovoj zhidkosti. – Kol'covo, 2007. – 43 s. [In Russian].

Vel'kov VV, Reznikova OI. Sovremennaja laboratornaja diagnostika renal'nyh patologij: ot rannih stadij do ostroj pochechnoj nedostatochnosti. Laboratorna dіagnostika. 2010; 4 (54): 59-65. [In Russian].

Jahn T, Radford S. The Yinand Yang of protein folding. FEBSJournal. 2005; 272 (23): 5962-70.doi: 10.1111/j.1742-4658.2005.05021.

Zabolotnyi DI, Bielousova AO, Zarytska IS, ta inshi. Autokhtonna β-ahrehatsiia bilkiv: prychyny, molekuliarni mekhanizmy ta patolohichni naslidky. Zhurnal NAMN Ukrainy. 2014; 24 (4): 385-92. (In Ukrainian).

Hamley IW. Peptide fibrillization. Angew Chem Int Ed. 2007; 46 (43):8128-47.doi: 10.1002/anie.200700861.

Gertz MA. Immunoglobulin light chain amytloidosis: 2018 update on diagnosis, prognosis, and treatment. Am J Hematol.2018; 93 (9): 1169-80.doi: 10.1002/ajh.25149.

Sideras K. and Gertz M. Amyloidosis. Adv Clin Chem. 2009; 47: 1-44. PMID: 19634775. Available from:

Semerdzhiev SA, Dekker DR, Subramaniam V, Cklaessens MMAE. Self-assembly of protein fibrils into suprafibrillar aggregates: brindging the nano- and mesoscale. ACS Nano. 2014. 8(6): 5543-51.doi: 10.1021/nn406309c.

Sunde M, Serpell LC, Bartlam M, Fraser PE, Pepys MB, Balke CC. Common core structure of amyloids fibrils by synchrotron X-ray diffraction. JMolBiol. 1997; 273(3): 729-39.doi: 10.1006/jmbi.1997.1348.

Koga T, Taguchi K, Kogiso M, Kobuke Y, Kinoshita T, Higuchi M. Amyloid formation of native folded protein induced by peptide-based graft copolymer. FEBS Lett.2002; 531 (2): 137-40.PMID: 12417301.doi: 10.1016/S0014-5793(02)03438-5

Smirnov VP, Fadeev MJu. Bolezninakoplenija (tezaurisomozy). N. Novnogod, Izd-vo NGMA, 2007. 104 s. [In Russian].

Verevka SV. Parametabolic β-Aggregation of proteins: familiar mechanisms with diverse sequels. In: Berhardt LV, editor. Advances in Medicine and Biology. New York: Nova Science Publishers; 2013. Vol. 72. p. 29-48. Available from:

Krebs MRH, Bromley EHC, Rogers SS, Donald AM. The mechanism of amyloid spherolite formation by bovine insulin. Biophys J. 2005; 88 (3): 2013-21. doi: 10.1529/biophysj.104.051896.

Tsvirinko IR, Voroshylova NM, Timchenko MD, Kruhlyk OV, Verevka SV. β-ahrehovani bilki v patolohichno zminenykh tkanynakh. VI. Osoblyvosti struktury bilka Bens-Dzhonsa ta obumovleni nymy diahnostychni mozhlyvosti. Laboratorna diahnostyka. 2018; 2 (81): 3-8.(In Ukrainian).

Zabolotnyi DI, Gogunskaya IV, Zabolotnaya DD, et al. Suicide antigens: induced denaturation of proteins in the development of allergic reactions. In: Berhardt LV, editor. Advances in Medicine and Biology. New York: Nova Science Publishers, 2012, Vol. 53, p.217-32. Available from:

Sapozhnikov SP, Karyshev PB, Sheptuhina AI, Nikolaeva OV, Avrujskaja AA, Mitrasov JuN, Kozlov VA. Novye fljuorescentnye zondy dlja vyjavlenija amiloida. Sovremennye tehnologii v medicine. 2017; 9 (2): 91-8.[In Russian].

Puchtler H, Sweat F, Levine M. On the binding of Congo red by amyloid. Journ Histochem Cytochem. 1962; 10: 355-64. doi: 10.1177/10.3.355

Kyle RA. Amyloidosis: a convoluted story. Historical review. Brit Journ Haematol.2001; 114 (3): 529-38.PMID: 11552976.doi: 10.1046/j.1365-2141.2001.02999.x

Brigger D, Muckle T. Comparison of Sirius red and Congo red as stains for amyloid in animal tissues. Journ Histochem Cytochem. 1975; 23 (1): 84-8.doi: 10.1177/23.1.46874.

Westermark GT, Westermark P.  Serum amyloid A and protein AA: molecular mechanisms of transmissible amyloidisis. FEBS Lett. 2009; 583 (16): 2685-90.doi: 10.1016/j.febslet.2009.04.026.

Buxbaum J, Linke R.  A molecular history of the amyloidosis. J. Mol. Biol. 2012; 421 (2-3): 142-59. doi: 10.1016/j.jmb.2012.01.024.

McCarthy F, Adetoba A, Gill C, Bramham K, Bertollacini M, Burton G, Girardi G, Seed P, Poston L, Chappell L. Urinary comgophilia in women with hypertensive disorders of pregnancy and preexisting proteinuria or hypertension. Am J Obst Gynecol. 2016; 215 (4): 1-7.doi: 10.1016/j.ajog.2016.04.041.

Beetham R. Detection of Bence-Jones protein in practice. Ann Clin Biochem. 2000; 37(5): 563-70.doi: 10.1258/0004563001899690.

Saeed SM, Fine G. Thioflavin-T for amyloid detection. Am J Chem Pathol.1967; 47(5): 588-593.PMID: 4164576. doi.10.1093/ajcp/47.5.588.

Lowry OH, Rosebrough NI, Farr AL, Randall RI. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193 (1): 265-275. PMID: 14907713. Available from:

Anders H-J, Schaefer L. Beyond tissue injury – damage associated molecular patterns, toll-like receptors, and inflammasomes also druve regeneration and fibrosis. JAmSocNephrol. 2014; 25 (7): 1387-1400.doi:  10.1681/ASN.2014010117.

Yildiz G, Andrade J, Engeseth NE, Feng H. Functionalizing soy protein nanoaggregates with pH-shifting and mano-thermo-sonication. J. Colloid Interface Sci. 2017; 505: 836-846. doi: 10.1016/j.jcis.2017.06.088

Kovalska V, Chernii S, Cherepanov S, Losytskyy M, Chernii V, Varzatskii O, Naumovets A, Yarmoluk S. The impact of binding of macrocyclic metal complexes on amyloid fibrillization of insulin and lysozyme. Journ Mol Recognit. 2017; 30 (8): e2622. doi: 10.1002/jmr.2622.

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How to Cite
Voroshylova, N. M., Timchenko, M. D., & Verevka, S. V. (2019). Bence-Jones protein as the form of nano-scaled β-stacked supramolecular aggregates. Ukrainian Journal of Nephrology and Dialysis, (1(61), 39-44.