In vitro antiaggregation and deaggregation potential of Rhizophora mucronata and its bioactive compound (+)- catechin against Alzheimer’s beta amyloid peptide (25–35)

References

• Kumar S, Okello EJ, Harris JR. Experimerntal inhibition of fibrillogenesis and neurotoxicity by amyloid-beta (Aβ) and other disease related peptides/proteins by plant extracts and herbal compounds. Subcell Biochem. 2012;65:295–326.10.1007/978-94-007-5416-4
   PubMedGoogle Scholar
• Bates KA, Verdile G, Li QX, Ames D, Hudson P, Masters CL, et al. Clearance mechanisms of Alzheimer’s amyloid-β peptide: implications for therapeutic design and diagnostic tests. Mol Psychiatry. 2009;14:469–86.10.1038/mp.2008.96
   PubMed Web of Science ®Google Scholar
• Gilbert BJ. The role of amyloid β; in the pathogenesis of Alzheimer’s disease – a review. J Clin Pathol. 2013;66:362–66.10.1136/jclinpath-2013-201515
   PubMed Web of Science ®Google Scholar
• Gauci AJ, Caruana M, Giese A, Scerri C, Vassallo N. Identification of polyphenolic compounds and black tea extract as potent inhibitors of lipid membrane destabilization by Abeta42 aggregates. J Alzheimers Dis. 2011;27:767–79.
   PubMed Web of Science ®Google Scholar
• Millucci L, Ghezzi L, Bernardini G, Santucci A. Conformations and biological activities of amyloid beta peptide 25–35. Curr Protein Pept Sci. 2010;11:54–67.10.2174/138920310790274626
   PubMed Web of Science ®Google Scholar
• Larini L, Joan-Emma S. Role of b-hairpin formation in aggregation: The self-assembly of the amyloid-b (25–35) peptide. Biophys J. 2012;103:576–86.10.1016/j.bpj.2012.06.027
   PubMed Web of Science ®Google Scholar
• Giordano M. Beta-amyloid protein (25–35) disrupts hippocampal network activity: role of Fyn-kinase. Hippocampus. 2010;20:78–96.
   PubMed Web of Science ®Google Scholar
• Syad AN, Devi KP. Assessment of anti-amyloidogenic activity of marine red alga G. acerosa against Alzheimer’s beta-amyloid peptide 25–35. Neurol Res. 2015;37:14–22.10.1179/1743132814Y.0000000422
   PubMed Web of Science ®Google Scholar
• Shanmuganathan B, Sheeja Malar D, Sathya S, Pandima Devi Kasi. Antiaggregation Potential of Padina gymnospora against the Toxic Alzheimer’s Beta-Amyloid Peptide 25–35 and Cholinesterase Inhibitory Property of Its Bioactive Compounds. PLOS One. 2015;10:e0141708.10.1371/journal.pone.0141708
   PubMed Web of Science ®Google Scholar
• Duke JA, Wain KK. Medicinal plants of the world. Computer index with more than 85,000 entries. In: Duke JA, editor. Handbook of medicinal herbs. Boca Raton, FL: CRC press; 1981. p. 96.
   Google Scholar
• Bandaranayake WM. Bioactivities, Bioactive compounds and chemical constituents of mangrove plants. Wetlands Ecol Manag. 2002;10:421–52.10.1023/A:1021397624349
   Google Scholar
• Liebezeit G, Rau MT. New Guinean mangroves – traditional usage and chemistry of natural products. Senckenbergiana maritime. 2006;36:1–10.10.1007/BF03043698
   Google Scholar
• Premanathan M, Arakaki R, Izumi H, Kathiresan K, Nakarno M, Yamamoto N, Nakashima H. Antiviral properties of a mangrove plant, Rhizophora apiculata blume, against human immunodeficiency virus. Antiviral Res. 1999;44:113–22.10.1016/S0166-3542(99)00058-3
   PubMed Web of Science ®Google Scholar
• Suganthy N, Pandian SK, Devi KP. Cholinesterase inhibitory effects of Rhizophora lamarckii, Avicennia officinalis, Sesuvium portulacastrum and Suevada monica: Mangroves inhabiting Indian coastal area (Vellar Estuary). J Enz Inhib Med Chem. 2008;24:702–07.
   Web of Science ®Google Scholar
• Suganthy N, Devi KP. In vitro antioxidant and anti-cholinesterase activities of Rhizophora mucronata. Pharm Biol. 2016;54:118–29.10.3109/13880209.2015.1017886
   PubMed Web of Science ®Google Scholar
• Suganthy N, Devi KP. Protective effect of catechin rich extract of Rhizophora mucronata against β-amyloid-induced toxicity in PC12 cells. J Appl Biomed. 2016;14:137–46.10.1016/j.jab.2015.10.003
   Web of Science ®Google Scholar
• Suganthy N, Sheeja Malar D, Devi KP. Rhizophora mucronata attenuates beta-amyloid induced cognitive dysfunction, oxidative stress and cholinergic deficit in Alzheimer’s disease animal model. Metabol Brain Dis. 2016;31:937–949.10.1007/s11011-016-9831-0
   PubMed Web of Science ®Google Scholar
• Ramesh BN, Indi SS, Rao KSJ. Anti-amyloidogenic property of leaf aqueous extract of Caesalpinia crista. Neurosci Lett. 2010;475:110–4.10.1016/j.neulet.2010.03.062
   PubMed Web of Science ®Google Scholar
• Khurana R, Coleman C, Ionescu-Zanetti C, Carter SA, Krishna V, Grover RV, et al. Mechanism of thioflavin T binding to amyloid fibrils. J Struct Biol. 2005;151:229–38.10.1016/j.jsb.2005.06.006
   PubMed Web of Science ®Google Scholar
• Munoz-Ruiz P, Rubio L, Garcia-Palomero E, Dorronsoro I, del MonteMillan M, Valenzuela R, et al. Design, synthesis, and biological evaluation of dual binding site acetyl cholinesterase inhibitors: new disease-modifying agents for Alzheimer’s disease. J Med Chem. 2005;48:7223–33.10.1021/jm0503289
   PubMed Web of Science ®Google Scholar
• Klunk WE, Jacob RF, Mason RP. Quantifying amyloid beta-peptide (Aβ) aggregation using congo red – Aβ spectrophotometric assay.Anal Biochem. 1999;266:66–76.10.1006/abio.1998.2933
   PubMed Web of Science ®Google Scholar
• Zandomeneghi G, Krebs MRH, Mccammon MG, Fandrich M. FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils. Protein Sci. 2004;13:3314–21.
   PubMed Web of Science ®Google Scholar
• Bolder SG, Sagis LM, Venema P, van der Linden E. Thioflavin T and birefringence assays to determine the conversion of proteins into fibrils. Langmuir. 2007;23:4144–7.10.1021/la063048k
   PubMed Web of Science ®Google Scholar
• Harper JD, Wong SS, Lieber CM, Lansbury PT. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem Biol. 1997;4:119–25.10.1016/S1074-5521(97)90255-6
   PubMed Web of Science ®Google Scholar
• Kuperstein I, Broersen K, Benilova I, Rozenski J, Jonckheere W, Debulpaep M, et al. Neurotoxicity of Alzheimer’s disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio. EMBO J. 2010;29:3408–20.10.1038/emboj.2010.211
   PubMed Web of Science ®Google Scholar
• Li H, Rahimi F, Sinha S, Maiti P, Bitan G, Murakami K. Amyloids and protein aggregation-analytical methods. In: Meyers RA, editor. Encyclopedia of analytical chemistry. New York: Wiley; 2009. p. 1–32.
   Google Scholar
• Kong J, Yu S. Fourier transform infrared spectroscopic analysis of protein Secondary structures. Acta Biochim Biophys Sin. 2007;39:549–59.
   Google Scholar
• Goormaghtigh E. FTIR data processing and analysis tools. In: Barth A, Haris P, editors. Advances in biomedical spectroscopy. Amsterdam: IOS Press; 2009. p. 104–28.
   Google Scholar
• Naldi M, Fiori J, Pistolozzi M, Drake AF, Bertucci C, Wu R, et al. Amyloid β-peptide 25–35 Self-assembly and its inhibition: a model undecapeptide system to gain atomistic and secondary structure details of the Alzheimer’s disease process and treatment. ACS Chem Neurosci. 2012;3:952–62.10.1021/cn3000982
   PubMed Web of Science ®Google Scholar
• Terzi E, Holzemann G, Seelig J. Reversible random coil β sheet transition of the Alzheimer β-Amyloid fragment. Biochemistry. 1994;33:1345–50.10.1021/bi00172a009
   PubMed Web of Science ®Google Scholar
• Yang SG, Wang WY, Ling TJ, Feng Y, Du XT, Zhang X, et al. α-Tocopherol quinone inhibits β-amyloid aggregation and cytotoxicity, disaggregates preformed fibrils and decreases the production of reactive oxygen species, NO and inflammatory cytokines. Neurochem Int. 2010;57:914–22.10.1016/j.neuint.2010.09.011
   PubMed Web of Science ®Google Scholar
• Ono K, Yoshiike Y, Takashima A, Hasegawa K, Naiki H, Yamada M. Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer’s disease. J Neurochem. 2003;87:172–81.10.1046/j.1471-4159.2003.01976.x
   PubMed Web of Science ®Google Scholar
• Grelle G, Otto A, Lorenz M, Frank RF, Wanker EE, Bieschke J. Black tea theaflavins inhibit formation of toxic amyloid-β and α-synuclein fibrils. Biochemistry. 2011;50:10624–36.10.1021/bi2012383
   PubMed Web of Science ®Google Scholar