Amyloid-&amp;beta; peptide (1&amp;ndash;42) aggregation induced by copper ions under acidic conditions

Bin, Yannan; Li, Xia; He, Yonghui; Chen, Shu; Xiang, Juan

doi:10.1093/abbs/gmt044

Cited by 35 publications

(16 citation statements)

References 43 publications

(56 reference statements)

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confidence: 99%

“…Yoshiike et al reported that positively charged Aβ fibrils/profibrils are highly cytotoxic, and neutralization of the charges could reduce neuronal toxicity [8] . Moreover, covalent modification of the charged amino groups of Aβ peptides through glycation and acylation could significantly reduce cytotoxicity of Aβ species [8a] . In addition, Yang et al showed that surface coating of Aβs with open-chain conjugates of polyether-thioflavin analogues could reduce the adhesion of Aβs towards Anti-Aβ IgG, and could ameliorate dendritic spine density and improve cognitive function in an AD mouse model [9] .…”

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confidence: 99%

“…Zeta potential has been used to evaluate the potential change between the double layer and the sliding plane of particles, and has also been used for studying interactions between amyloid fibrils and its ligands [8b, 12] . Our zeta-potential test suggested that 12-crown-4 ether could change the surface charges of Aβs.…”

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confidence: 99%

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Crown ethers attenuate aggregation of amyloid beta of Alzheimer's disease

Tian

Zhang

et al. 2014

Chem. Commun.

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The stagnant state of drug development for Alzheimer’s disease demands new approaches for seeking promising candidates. In this report, we reasoned that non-covalent modification of amyloid beta (Aβ) peptide by crown ethers could inhibit its aggregation. To specifically target Aβs, a conjugate of Pittsburgh compound B (PiB) and 12-crown-4 ether (termed PiB-C) was synthesized. Our results indicated that the conjugate could significantly reduce the aggregation of Aβs in vitro. In addition, by two-photon microscopic imaging, we found that PiB-C could readily penetrate the BBB and efficiently label Aβ plaques and CAAs (cerebral amyloid angiophathy) in an APP-PS1 transgenic mouse.

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confidence: 99%

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confidence: 99%

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Crown ethers attenuate aggregation of amyloid beta of Alzheimer's disease

Tian

Zhang

et al. 2014

Chem. Commun.

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“…Detailed analysis has shown that Cu(II) hinders the formation of the β-sheet while still promoting the aggregation of the peptide 283 , and in addition AFM and EM have shown that Cu(II) has a similar effect on other amyloid peptides. When human islet amyloid polypeptide is incubated with Cu(II) fibrillisation is suppressed but the population of aggregates is smaller, and increased ROS over-production and mitochondrial dysfunction are noted 283 .…”

Section: Resultsmentioning

confidence: 99%

Nanoscale Imaging and Characterisation of Amyloid-β

Tinker-Mill¹

2016

Springer Theses

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I am blessed to have made so many friends throughout this PhD; both within the university and elsewhere. Jenny Mayes and Alex Robson, thank you for brightening my morning with many a cup of coffee and chatter, in addition to all your support with my research. Riccardo Mazzocco, who will always be "my favourite Italian". Kylie O'Shea and Ben Shreeve, without whom I would not have enjoyed nearly as much cake as I have currently. The wonderful Taylor Lura, Emily Smith and Christie Herd, who have made me laugh so hard I have cried. My "Bookend" Louise Walker for fostering my madness and creating the candyfloss world with me. I would like to thank Dr. Christine Shirras for her guidance and support as my teaching mentor. Lastly, my friends in Canada; Ronnie and Liz Drolle, who I would never have had the joy of meeting if it were not for this PhD. All of these people, and more, have made this experience the happiest of my life. You've brought so much joy, sparkle and laughter as we've journeyed together. I'm so lucky to have you in my life. My family's support and belief in me has been paramount throughout my studies, and I thank them from the bottom of my heart of believing in me, comforting me and giving me the strength I have. Most importantly I want to thank my long-suffering husband, Richard. Without you I would not be me, and this would not have happened. We share this achievement as we do everything. I love you now, forever and always and cannot thank you enough for your support and love. IV Dedications The work in this thesis is dedicated to those that sadly did not get the opportunity to see me finish this journey, but offered their unconditional support and love throughout my life. Vera Pennington, who sadly lost her own battle with Alzheimer's disease inspired with her tireless work as a daughter, mother and grandmother. Rex Pennington, who went long before this journey began. Thank you for the memories. Marjorie and Ernest Tinker, without whom I would not have been able to begin this journey. I love and miss you both so much and am eternally grateful for all that you did for me. It breaks my heart you will not see me graduate. V

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“…A--beta binds 691 copper with high affinity, and demonstrates enzyme--like activity, oxidizing 692 cholesterol and reducing O2 to H202 (47). Copper induces Abeta aggregation 693 amorphously, and inhibits Beta--sheet structure formation (48 (33). Alpha--synuclein resides in lipid rafts and binds to GM1, promoting 717 oligomer formation (33).…”

Section: Transmissible Spongiform Encephalopathymentioning

confidence: 99%

Beyond the protein-only hypothesis: A novel mineral-lipid hypothesis in prion and protein-misfolding disease

Reddy

2017

Preprint

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A scientific theory or hypothesis is presented, in which mineral particles may play a pivotal role in the prion disease transmissible spongiform encephalopathy (TSE), and possibly also in other protein--misfolding diseases. Montmorillonite clay (Mte) and other minerals are known to bind to scrapie prion protein (PrP--Sc) in soil. The hypothesis is explored that, in transmissible spongiform encephalopathy, Mte or other mineral particles, upon contact with lipids, such as in the gut or at the cell plasma membrane, may interact with lipids or with lipid rafts. The minerals may catalyze formation of lipid vesicles, and might also be capable of inducing lipid raft clustering or other lipid raft or plasma membrane changes. Some of these lipid vesicles or rafts might then contain or bind PrP--Sc, and sometimes also contain montmorillonite or the mineral catalyst. Mte--PrP--Sc or the affected lipid vesicles/particles could also promote PrP--C to PrP--Sc conversion by providing conditions for misfolding. These conditions provided for protein misfolding may include the following: multiple unique compartments providing sizes, shapes or aqueous/lipid environments that promote varied folding conformations, presence of an anion (Mte), negative--charge (Mte), lipid membrane mimetic (e.g. associated lipid particle, vesicle or raft), interaction with bound or contained PrP--Sc, presence of bound copper, and/or copper binding affinity. Mte--catalyzed lipid vesicles are proto--cell--like entities, making them potential candidates to be part of the infectious particle in prion disease, which can behave like an infectious organism but does not appear to depend on nucleic acid. Lipid vesicles or rafts may resemble endosomes, which would be consistent with reports of prion being transported and formed along an endosome--like pathway. Additionally, the vesicles or rafts could accumulate intra--cellularly, and might form tubulovesicular structures, which are hallmarks of prion disease. Potential applications of this theory to more common protein misfolding diseases, Alzheimer's disease, Parkinson's disease, and Amyotrophic lateral sclerosis, are discussed. This theory, which I term the mineral--lipid prion hypothesis, provides a basis for potential novel interventions in the field of prion and protein--misfolding diseases. In addition, this theory suggests that similar silicate--or mineral--catalyzed lipid vesicles/liposomes might be further explored as useful compartments that could be manipulated in order to deliver molecules or even proteins to or from cells.PeerJ Preprints | https://doi.org/10.7287/peerj.preprints.2982v1 | CC BY 4.0

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Amyloid-β peptide (1–42) aggregation induced by copper ions under acidic conditions

Cited by 35 publications

References 43 publications

Crown ethers attenuate aggregation of amyloid beta of Alzheimer's disease

Crown ethers attenuate aggregation of amyloid beta of Alzheimer's disease

Nanoscale Imaging and Characterisation of Amyloid-β

Beyond the protein-only hypothesis: A novel mineral-lipid hypothesis in prion and protein-misfolding disease

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