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  3. Vol. 4 No. 2 (2018): Spring
  4. Research/Original Article- Immunology

Vol. 4 No. 2 (2018)

October 2019

Investigating the inhibitory effects of Seidlitzia rosmarinus extract on the amyloid fibril formation of ҡ-casein in the presence of dextran

  • Arezou Ghahghaei
  • Khatoon Heidari nasab
  • Fariba Mohammadi Tahroodi
  • shohreh rahimi

Archives of Medical Laboratory Sciences, Vol. 4 No. 2 (2018), 13 October 2019 , Page 30-36
https://doi.org/10.22037/amls.v4i2.25212 Published: 2019-10-14

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Abstract

Background: Formation of amyloid fibrils has been associated with different protein aggregation diseases. Many studies indicate that many proteins can be converted in vitro into amyloid structures. Isolated ҡ-casein (ҡ-CN) spontaneously forms amyloid fibrils under physiological conditions, so it is a convenient model for researching generic aspect of fibril formation.

Materials and Methods: In this study the effect of aqueous extract of S. rosmarinus on the amyloid formation of ҡ-CN in the presence and absence of crowding agent, dextran, have been examined using Thioflavin T binding (ThT) assay, fluorescence spectroscopy, and circular dichroism (CD) spectroscopy.

Results: ThT binding assay showed that dextran increased the rate of amyloid fibril formation and S. rosmarinus extract retarded the amyloid fibril formation in κ-CN. In the presence of dextran however, the effect of   S. rosmarinus extract on the amyloid formation of ҡ-CN was less than in its absence.

Fluorescence spectroscopy results also demonstrated that dextran led to unfolding and increased the exposure hydrophobic area in ҡ-CN. S. rosmarinus extract efficiency decreased the exposure of hydrophobic regions in κ-CN, whereas in the presence of dextran this effect of extract was reduced.

CD spectroscopy results exhibited that incubation of κ-CN with S. rosmarinus extract prevented a structural transition to a β-sheet. CD spectroscopy results also indicated that by adding dextran to reduced κ-CN β-sheet structures observed, which indicates structural change. S. rosmarinus extract however, prevented transition to β-sheet structural.

Conclusion: In conclusion our finding suggests that S. rosmarinus extract prevents amyloid fibril formation in κ-CN, although this effect decreased in the presence of dextran.
Keywords:
  • S. rosmarinus
  • ҡ-casein
  • Aggregation
  • amyloid.
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How to Cite

1.
Ghahghaei A, Heidari nasab K, Mohammadi Tahroodi F, rahimi shohreh. Investigating the inhibitory effects of Seidlitzia rosmarinus extract on the amyloid fibril formation of ҡ-casein in the presence of dextran. Arch Med Lab Sci [Internet]. 2019 Oct. 14 [cited 2026 Jun. 30];4(2):30-6. Available from: https://journals.sbmu.ac.ir/index.php/medlab/article/view/25212
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References

Dobson CM. Experimental investigation of protein folding and misfolding. Methods. 2004;34(1),4-14.

Rochet JC, Lansbury PT JR. Amyloid fibrillogenesis: Themes and variations. Current Opinion in Structural Biology. 2000;10(1), 60-68.

Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature. 1997;385(6619),787-793.

Ecroyd H, Koudelka T, Thorn DC, Williams DM, Devlin G, Hoffmann P, et al. Dissociate from the oligomeric state is the Rate-limiting step in fibril formation by κ-casein, The Journal of Biological Chemistry. 2008;283(14),9012-9022.

Breckle SW. Studies on halophytes from Iran and Afghanistan. II* Ecology of halophytes salt gradients. Cambridge University Press. 1986;203-215.

Hadi MR. Biotechnological potentials of seidlitzia rosmarinus: a mini review. African Journal of Biotechnology. 2009;8(11)2429-2431.

Caballero B, Trugo LC, Finglas PM. Encyclopedia of Food Sciences and Nutrition, 2nd Edition. Academic Press. 2003;3082-3090.

Niewold TA, Murphy CL, Hulskamp-Koch CA, Tooten PC, Gruys E. Casein related amyloid characterization of a new and unique amyloid protein isolated from bovine corpora amylacea. Amyloid: International Journal of Experimental & Clinical Investigation Amyloid. 1999;6,244-249.

Panouile M, Nicolai T, Durand D. Heat induced aggregation and gelation of casein submicelles. International Dairy Journal. 2004;14(4),297-303.

Rasmussen LK, Johnsen LB, Tsiora A, Sorensen ES. Disulphide-linked caseins and micelles. 1999;9(3),215-218.

Ghahghaei A, Shafiibafti E, 0-Structural Study of κ-casein During Amyloid Formation at Different Temperature. Australian Journal of Basic and Applied Sciences. 2010;4(8),2257-2266.

Farell HM Jr, Cooke PH, Wickham ED, Piotrowski EG, Hoagland PD. Environmental influences on bovine κ-casein: reduction and conversion to fibrillary (amyloid) structure, Journal of protein chemistry. 2003;22(3),259-273.

Thorn DC, Meehan S, Sunde M, Rekas A, Gras SL, MacPhee CE, et al. Amyloid fibril formation by bovine milk κ-casein and its inhibition by the molecular chaperones αs- and β-casein. Biochemistry. 2005;44(51),17027-17036.

Heidari AA, Ghahghaei A, Valizadeh J. Evaluation of chaperone ability of S. rosmarinus against protein aggregation, Journal of Pharmaceutical Investigation. 2014;44,423-430.

Rasmussen LK, Hojrup P, Petersen TE. The multimeric structure and disulfide-bonding pattern of bovine κ-casein, FEBS Jornal. 1992;207(1), 215-222.

Fox PF, McSweeney PLH. chemistry of the caseins. Advanced Dairy Chemistry. 2003;1,Part A,139-201.

Fasman GD. Aromatic and cystine side-chain circular Dichroism in proteins. Circular Dichroism and the conformational analysis of biomolecules. Plenum Press, New York. 1996;18, 109–157.

Breydo L, Reddy KD, Piai A, Felli IC, Pierattelli R, Uversky VN. The crowd you're in with: Effects of different types of crowding agents on protein aggregation, Biochimica et Biophysica Acta. 2014;1844(2),346-357.

Leonil J, Henry G, Jouanneau D, Delage MM, Forge V, Putaux JL. Kinetics of fibril formation of Bovine κ-casein Indicate a conformational rearrangement as a critical step in the process. Journal Molecular Biology. 2008;381(5), 1267–1280.

Lencki RW. Evidence for Fibril-like structure in bovine casein micelles. Journal of Dairy Science. 2007;90(1),75–89.

Porat Y, Abramowitz A, Gazit E. Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism, Chemical Biology Drug Design. 2006; 67(1),27–37.

Ghahghaei A, Mohammadi Dareh mianeh M. Investigating the chaperone activity of b-casein in preventing amyloid formation in j-casein in the presence of dextran. Journal of Pharmaceutical Investigation. 2015;45(5),407–413.

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