Bacoside-A, an anti-amyloid natural substance, inhibits membrane disruption by the amyloidogenic determinant of prion protein through accelerating fibril formation
Open accessAbstract
Bacosides, class of compounds extracted from the Bacopa monniera plant, exhibit interesting therapeutic properties, particularly enhancing cognitive functions and putative anti-amyloid activity. We show that bacoside-A exerted significant effects upon fibrillation and membrane interactions of the amyloidogenic fragment of the prion protein [PrP(106-126)]. Specifically, when co-incubated with PrP(106-126), bacoside-A accelerated fibril formation in the presence of lipid bilayers and in parallel inhibited bilayer interactions of the peptide aggregates formed in solution. These interesting phenomena were studied by spectroscopic and microscopic techniques, which suggest that bacoside A-promoted fibrillation reduced the concentration of membrane-active pre-fibrillar species of the prion fragment. This study suggests that induction of fibril formation and corresponding inhibition of membrane interactions are likely the underlying factors for ameliorating amyloid protein toxicity by bacoside-A.
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Bacoside-A has notable impacts on the fibrillation process and membrane interactions of the amyloidogenic fragment of the prion protein (PrP(106-126)).
“Our findings indicate that bacoside-A has notable impacts on the fibrillation process and membrane interactions of the amyloidogenic fragment of the prion protein (PrP(106-126)).”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [127]
Bacoside-A expedites fibril formation in presence of lipid bilayers and impedes interactions of peptide aggregates with bilayers in solution when coincubated with PrP(106-126).
“Specifically, when coincubated with PrP(106-126), bacoside-A expedites the formation of fibrils in the presence of lipid bilayers while simultaneously impeding the interactions of the peptide aggregates with the bilayers formed in solution.”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [127]
Bacosides enhance cognitive functions and potentially exhibit anti-amyloid activity.
“Bacosides, a group of compounds derived from the BM plant, demonstrate noteworthy therapeutic characteristics, particularly in enhancing cognitive functions and potentially exhibiting anti-amyloid activity.”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [127]
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Cites
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,435 · see citing works
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Molecular mechanism of Thioflavin-T binding to amyloid fibrils
Biancalana, M., & Koide, S. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.04.001 · Cited by 2,203 · see citing works
The Amyloid State of Proteins in Human Diseases
Eisenberg, D. S., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,732 · see citing works
Kayed, R., Sokolov, Y., Edmonds, B. W., McIntire, T. M., Milton, S. C. F., Hall, J. E., & Glabe, C. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400260200 · Cited by 903 · see citing works
Prion-like mechanisms in neurodegenerative diseases
Frost, B., & Diamond, M. I. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2786 · Cited by 776 · see citing works
The binding of thioflavin-T to amyloid fibrils: localisation and implications
Krebs, M. R. H., Bromley, E. H. C., & Donald, A. M. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.08.002 · Cited by 756 · see citing works
Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils
Bieschke, J., Herbst, M., Wiglenda, T., Friedrich, R. P., Boeddrich, A., Schiele, F., Kleckers, D., del Amo, J. M. L., Grüning, B. A., Wang, Q., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.719 · Cited by 443 · see citing works
Levin, A., Mason, T. O., Adler‐Abramovich, L., Buell, A. K., Meisl, G., Galvagnion, C., Bram, Y., Stratford, S. A., Dobson, C. M., Knowles, T. P. J., et al. (2014) · Nature Communications · doi:10.1038/ncomms6219 · Cited by 277 · see citing works
Self-citationThe role of lipid–protein interactions in amyloid-type protein fibril formation
Gorbenko, G. P., & Kinnunen, P. K. J. (2006) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2006.02.006 · Cited by 267 · see citing works
Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro.
Tagliavini, F., Prelli, F. C., Verga, L., Giaccone, G., Sarma, R., Gorevic, P. D., Ghetti, B. F., Passerini, F., Ghibaudi, E. M., & Forloni, G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9678 · Cited by 243 · see citing works
Cheon, M., Chang, I., Mohanty, S., Luheshi, L. M., Dobson, C. M., Vendruscolo, M., & Favrin, G. (2007) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030173 · Cited by 212 · see citing works
Limpeanchob, N., Jaipan, S., Rattanakaruna, S., Phrompittayarat, W., & Ingkaninan, K. (2008) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2008.07.039 · Cited by 206 · see citing works
How Epigallocatechin Gallate Can Inhibit α-Synuclein Oligomer Toxicity in Vitro
Lorenzen, N., Nielsen, S. B., Yoshimura, Y., Vad, B. S., Andersen, C. B., Betzer, C., Kaspersen, J. D., Christiansen, G., Pedersen, J. S., Jensen, P. H., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554667 · Cited by 202 · see citing works
Binding of prion protein to lipid membranes and implications for prion conversion
Sanghera, N., & Pinheiro, T. J. T. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5322 · Cited by 186 · see citing works
Stefani, M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07889.x · Cited by 183 · see citing works
Jobling, M. F., Stewart, L. R., White, A. R., McLean, C., Friedhuber, A. M., Maher, F., Beyreuther, K. T., Masters, C. L., Barrow, C. J., Collins, S. J., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0731557.x · Cited by 174 · see citing works
Structural Changes of the Prion Protein in Lipid Membranes Leading to Aggregation and Fibrillization
Kazlauskaite, J., Sanghera, N., Sylvester, I., Vénien‐Bryan, C., & Pinheiro, T. J. T. (2003) · Biochemistry · doi:10.1021/bi026872q · Cited by 161 · see citing works
Bacopa monniera extract reduces amyloid levels in PSAPP mice
Holcomb, L. A., Dhanasekaran, M., Hitt, A. R., Young, K. A., Riggs, M., & Manyam, B. V. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9303 · Cited by 156 · see citing works
Kinetics of amyloid formation and membrane interaction with amyloidogenic proteins
Murphy, R. M. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.12.014 · Cited by 153 · see citing works
Fosse, J., Seegers, H. H., & Magras, C. (2007) · Veterinary Research · doi:10.1051/vetres:2007039 · Cited by 142 · see citing works
Brender, J., Dürr, U., Heyl, D., Budarapu, M. B., & Ramamoorthy, A. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.07.001 · Cited by 141 · see citing works
Membrane interactions of ionic liquids: Possible determinants for biological activity and toxicity
Gal, N., Malferrari, D., Kolusheva, S., Galletti, P., Tagliavini, E., & Jelinek, R. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2012.07.025 · Cited by 128 · see citing works
Self-citationPrion diseases — close to effective therapy?
Cashman, N. R., & Caughey, B. W. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1525 · Cited by 118 · see citing works
Cecchi, C., & Stefani, M. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.06.003 · Cited by 115 · see citing works
Membrane analysis with amphiphilic carbon dots
Nandi, S., Malishev, R., Kootery, K. P., Mirsky, Y., Kolusheva, S., & Jelinek, R. (2014) · Chemical Communications · doi:10.1039/c4cc03504f · Cited by 92 · see citing works
Self-citationSmall Liposomes Accelerate the Fibrillation of Amyloid β (1–40)
Terakawa, M. S., Yagi, H., Adachi, M., Lee, Y., & Goto, Y. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592527 · Cited by 87 · see citing works
Apetz, N., Münch, G. W., Govindaraghavan, S., & Gyengési, E. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140917110635 · Cited by 72 · see citing works
Cordeiro, Y., Lima, L. M. T. R., Gomes, M. P. B., Foguel, D., & Silva, J. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312262200 · Cited by 54 · see citing works
Dupiereux-Fettweis, I., Zorzi, W., Lins, L., Brasseur, R., Colson, P., Heinen, E., & Elmoualij, B. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.012 · Cited by 40 · see citing works
Lipid-Bilayer Dynamics Probed by a Carbon Dot-Phospholipid Conjugate
Nandi, S., Malishev, R., Bhunia, S. K., Kolusheva, S., Jopp, J., & Jelinek, R. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.04.005 · Cited by 40 · see citing works
Self-citationMiura, T., Yoda, M., 高久, 直., Hirose, T., & Takeuchi, H. (2007) · Biochemistry · doi:10.1021/bi700939j · Cited by 34 · see citing works
Morphology and Secondary Structure of Stable β-Oligomers Formed by Amyloid Peptide PrP(106−126)
Walsh, P. J., Yau, J., Simonetti, K., & Sharpe, S. J. (2009) · Biochemistry · doi:10.1021/bi9007319 · Cited by 31 · see citing works
Detection and Characterization of Membrane Microheterogeneity by Resonance Energy Transfer
Loura, L. M. S., de Almeida, R. F. M., & PRIETO, M. J. E. (2001) · Journal of Fluorescence · doi:10.1023/a:1012249117580 · Cited by 31 · see citing works
Toxicity Inhibitors Protect Lipid Membranes from Disruption by Aβ42
Malishev, R., Nandi, S., Kolusheva, S., Levi‐Kalisman, Y., Klärner, F., Schrader, T. H., Bitan, G., & Jelinek, R. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00200 · Cited by 30 · see citing works
Self-citationLipid bilayers significantly modulate cross-fibrillation of two distinct amyloidogenic peptides.
Gal, N., Morag, A., Kolusheva, S., Winter, R., Landau, M., & Jelinek, R. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4070427 · Cited by 29 · see citing works
Self-citationPhospholipid-Induced Fibrillation of a Prion Amyloidogenic Determinant at the Air/Water Interface
Dorosz, J., Volinsky, R., Bazar, E., Kolusheva, S., & Jelinek, R. (2009) · Langmuir · doi:10.1021/la901750v · Cited by 23 · see citing works
Self-citationMisfolding of the prion protein: linking biophysical and biological approaches
Noinville, S., Chich, J., & Rezaei, H. (2008) · Veterinary Research · doi:10.1051/vetres:2008025 · Cited by 17 · see citing works
Gal, N., Kolusheva, S., Kedei, N., Telek, A., Naeem, T. A., Lewin, N. E., Lim, L., Mannan, P., Garfield, S. H., Kazzouli, S. E., et al. (2011) · ChemBioChem · doi:10.1002/cbic.201100246 · Cited by 10 · see citing works
Self-citationAggregation of Beta-Amyloid Peptides Proximal to Zwitterionic Lipid Bilayers.
Yang, C.-I., Tsai, B., Huang, S.-J., Wang, T.-Y., Tai, H.-C., & Chan, J. C. (2015) · Chemistry - An Asian Journal · doi:10.1002/asia.201500482 · Cited by 8 · see citing works
DMPC: A Remarkable Exception to the Tocopherol's Membrane Presence
Marquardt, D., Williams, J. A., Kinnun, J. J., Kučerka, N., Atkinson, J., Wassall, S. R., Katsaras, J., & Harroun, T. A. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2013.11.304 · Cited by 2 · see citing works
PRION PROTEIN AS A PATHOGEN: A REVIEW
Nimiwal, B. K., Jalandhra, M. K., Sharma, M., & Thacker, P. S. (2012) · International Journal of Biomedical and Advance Research · doi:10.7439/ijbar.v3i7.574 · Cited by 2 · see citing works
Côté, S., Binette, V., Salnikov, E. S., Bechinger, B., Wei, G., & Mousseau, N. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2013.11.621 · Cited by 1 · see citing works
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Research works printed but not linked: 1
- S.R. Bammidi, S.S. Volluri, S.C. Chippada, S. Avanigadda, M. Vangalapati, A review on pharmacological studies of Bacopa monniera, J. Chem. Biol. Phys. Sci. (JCBPS) 1 (2011) 250.
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- Authors
- Malishev, R., Nandi, S., Kolusheva, S., Shaham-Niv, S., Gazit, E., & Jelinek, R.
- Affiliations
- Ben-Gurion University of the Negev (IL)
- Tel Aviv University (IL)
- Corresponding author
- Jelinek, Raz
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 1858
- Issue
- 9
- Pages
- 2208-2214
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2460324495
- Cited by
- 21
- References
- 44
- Citations by year
- 2026: 1 · 2023: 4 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 5 · 2018: 4 · 2017: 3
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 365 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- bacoside A, Bacopa monnieri, prion protein, amyloid fibril formation, membrane damage, lipid bilayers, amyloid toxicity, anti-amyloid activity, phytochemicals
- MeSH terms
- Prion Proteins, Amyloid, Membranes, Artificial, Saponins, Triterpenes
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