It is well known that misfolded peptides/proteins can play a role in processes of normal ageing and in the pathogenesis of many diseases including Alzheimer's disease. Previously, we evaluated samples of cerebrospinal fluid from patients with Alzheimer's disease and multiple sclerosis by means of thioflavin-T-based fluorescence. We observed attenuated effects of magnetite nanoparticles operated via anti-aggregation actions on peptides/proteins from patients with Alzheimer's disease but not from those with multiple sclerosis when compared to age-related controls. In this study, we have evaluated the in vitro effects of anti-aggregation operating ferrofluid and phytoalexin spirobrassinin in the cerebrospinal fluid of patients with multiple sclerosis and Alzheimer's disease. We have found significant differences in native fluorescence (λ excitation = 440 nm, λ emission = 485 nm) of samples among particular groups (young controls < multiple sclerosis, Alzheimer's disease < old controls). Differences among groups were observed also in thioflavin-T-based fluorescence (young controls = multiple sclerosis < Alzheimer's disease < old controls) and the most marked change from native to thioflavin-T-based fluorescence was found in young controls (28-40 years old people). Both ferrofluid and spirobrassinin evoked drops in thioflavin-T-based fluorescence; however, ferrofluid was more efficient in old controls (54-75 years old people) and spirobrassinin in multiple sclerosis patients, both compared to young controls. The results are discussed especially in relation to aggregated peptides/proteins and liposoluble fluorescent products of lipid peroxidation. Based on the significant effect of spirobrassinin in vitro, we suggest that spirobrassinin may be of therapeutic value in multiple sclerosis.

Prague Psychiatric Centre Alzheimer Disease Centre Ustavni 91 181 03 Prague 8 Bohnice Czech Republic

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Drugs Exp Clin Res. 1998;24(3):125-31 PubMed

Exp Toxicol Pathol. 2012 Jan;64(1-2):51-6 PubMed

Ann Neurol. 2001 Jul;50(1):121-7 PubMed

Brain Res Rev. 2006 Sep;52(2):316-26 PubMed

J Neurol. 2004 Mar;251(3):261-8 PubMed

Nanotechnology. 2012 Feb 10;23(5):055101 PubMed

Eur J Neurol. 2009 Jun;16(6):760-70 PubMed

Exp Parasitol. 2009 May;122(1):66-9 PubMed

J Biol Chem. 1996 Apr 26;271(17):10169-74 PubMed

Int J Clin Pharmacol Res. 1994;14(4):119-23 PubMed

Biomed Opt Express. 2010 Dec 06;2(1):71-9 PubMed

Phytochemistry. 2006 Jul;67(14):1503-9 PubMed

Anal Chem. 1994 Oct 15;66(20):3512-8 PubMed

Br J Pharmacol. 2006 Apr;147(8):873-85 PubMed

J Neurochem. 2008 Jan;104(2):457-68 PubMed

Lancet Neurol. 2005 Jan;4(1):32-41 PubMed

J Chem Biol. 2010 Mar;3(1):1-18 PubMed

Exp Gerontol. 2001 Sep;36(9):1539-50 PubMed

Anal Chem. 1999 Nov 1;71(21):4997-5002 PubMed

Mol Biosyst. 2010 Nov;6(11):2200-5 PubMed

Nat Prod Rep. 2009 Mar;26(3):382-445 PubMed

Biophys J. 2005 Jun;88(6):4200-12 PubMed

Pharm Res. 2008 Jul;25(7):1487-99 PubMed

Proteins. 2013 Jun;81(6):994-1004 PubMed

J Neurol Sci. 2012 Oct 15;321(1-2):49-53 PubMed

World J Biol Psychiatry. 2005;6(2):69-84 PubMed

Mol Biosyst. 2009 Oct;5(10):1174-9 PubMed

Alzheimers Dement. 2011 May;7(3):263-9 PubMed

Neurochem Res. 2012 Dec;37(12):2706-14 PubMed