Effects of zinc and carnosine on aggregation kinetics of Amyloid-β40 peptide

Tanzi, 2005, Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective, Cell, 120, 545, 10.1016/j.cell.2005.02.008 M Grabrucker, 2011, Brain-delivery of zinc-ions as potential treatment for neurological diseases: mini review, Drug Deliv. Lett., 1, 13 Markesbery, 1984, Brain trace element concentrations in aging, Neurobiol. Aging, 5, 19, 10.1016/0197-4580(84)90081-2 Takeda, 2000, Relationship between brain zinc and transient learning impairment of adult rats fed zinc-deficient diet, Brain Res., 859, 352, 10.1016/S0006-8993(00)02027-8 Miller, 2006, Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer's disease, J. Struct. Biol., 155, 30, 10.1016/j.jsb.2005.09.004 Lovell, 1998, Copper, iron and zinc in Alzheimer's disease senile plaques, J. Neurol. Sci., 158, 47, 10.1016/S0022-510X(98)00092-6 Minicozzi, 2008, Identifying the minimal copper-and zinc-binding site sequence in amyloid-β peptides, J. Biol. Chem., 283, 10784, 10.1074/jbc.M707109200 Nair, 2010, NMR studies of zinc, copper, and iron binding to histidine, the principal metal ion complexing site of amyloid-β peptide, J. Alzheim. Dis., 20, 57, 10.3233/JAD-2010-1346 Yoshiike, 2001, New insights on how metals disrupt amyloid β-aggregation and their effects on amyloid-β cytotoxicity, J. Biol. Chem., 276, 32293, 10.1074/jbc.M010706200 Abelein, 2015, Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation, Proc. Natl. Acad. Sci. U.S.A., 112, 5407, 10.1073/pnas.1421961112 Bush, 1994, Rapid induction of Alzheimer Aβ amyloid formation by zinc, Science, 265, 1464, 10.1126/science.8073293 Guo, 2017, Kinetic insights into Zn2+-induced amyloid β-protein aggregation revealed by stopped-flow fluorescence spectroscopy, J. Phys. Chem. B, 121, 3909, 10.1021/acs.jpcb.6b12187 Lee, 2018, Zinc ion rapidly induces toxic, off-pathway amyloid-β oligomers distinct from amyloid-β derived diffusible ligands in Alzheimer's disease, Sci. Rep., 8, 1 Tõugu, 2009, Zn (II)‐and Cu (II)‐induced non‐fibrillar aggregates of amyloid-β (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators, J. Neurochem., 110, 1784, 10.1111/j.1471-4159.2009.06269.x Miller, 2010, Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states, Proc. Natl. Acad. Sci. U.S.A., 107, 9490, 10.1073/pnas.0913114107 Boldyrev, 2013, Physiology and pathophysiology of carnosine, Physiol. Rev., 93, 1803, 10.1152/physrev.00039.2012 Gariballa, 2000, Carnosine: physiological properties and therapeutic potential, Age Ageing, 29, 207, 10.1093/ageing/29.3.207 Reddy, 2005, Carnosine: a versatile antioxidant and antiglycating agent, Sci. Aging Knowl. Environ., 18 Corona, 2011, Effects of dietary supplementation of carnosine on mitochondrial dysfunction, amyloid pathology, and cognitive deficits in 3xTg-AD mice, PLoS One, 6, 10.1371/journal.pone.0017971 Kawahara, 2011, Zinc, copper, and carnosine attenuate neurotoxicity of prion fragment PrP106-126, Metallomics, 3, 726, 10.1039/c1mt00015b Attanasio, 2013, Carnosine inhibits Aβ42 aggregation by perturbing the H-bond network in and around the central hydrophobic cluster, Chembiochem, 14, 583, 10.1002/cbic.201200704 Caruso, 2019, Carnosine prevents Aβ-induced oxidative stress and inflammation in microglial cells: a key role of TGF-β1, Cells, 8, 64, 10.3390/cells8010064 Morris, 2018, N-Terminal charged residues of amyloid-beta peptide modulate amyloidogenesis and interaction with lipid membrane, Chem. Eur J., 24, 9494, 10.1002/chem.201801805 Liu, 2015, Site-specific dynamics of amyloid formation and fibrillar configuration of Aβ 1–23 using an unnatural amino acid, Chem. Commun., 51, 7000, 10.1039/C5CC00149H Micsonai, 2015, Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy, Proc. Natl. Acad. Sci. U.S.A., 112, E3095, 10.1073/pnas.1500851112 Nick, 2018, A long‐lived Aβ oligomer resistant to fibrillization, Biopolymers, 109, 10.1002/bip.23096 Fu, 2015, Mechanism of nucleated conformational conversion of Aβ42, Biochemistry, 54, 4197, 10.1021/acs.biochem.5b00467 Hasecke, 2018, Origin of metastable oligomers and their effects on amyloid fibril self-assembly, Chem. Sci., 9, 5937, 10.1039/C8SC01479E Hasecke, 2021, Protofibril–fibril interactions inhibit amyloid fibril assembly by obstructing secondary nucleation, Angew. Chem. Int. Ed., 60, 3016, 10.1002/anie.202010098 Banerjee, 2021, Carnosine improves aging-induced cognitive impairment and brain regional neurodegeneration in relation to the neuropathological alterations in the secondary structure of amyloid beta (Aβ), J. Neurochem., 158, 710, 10.1111/jnc.15357 Attanasio, 2009, Protective effects of L-and D-carnosine on α-crystallin amyloid fibril formation: implications for cataract disease, Biochemistry, 48, 6522, 10.1021/bi900343n Aloisi, 2013, Anti-aggregating effect of the naturally occurring dipeptide carnosine on Aβ1-42 fibril formation, PLoS One, 8, 10.1371/journal.pone.0068159 Brown, 1979, Chelation chemistry of carnosine. Evidence that mixed complexes may occur in vivo, J. Phys. Chem., 83, 3314, 10.1021/j100489a002 Matsukura, 1990, Characterization of crystalline L-carnosine Zn (II) complex (Z-103), a novel anti-gastric ulcer agent: tautomeric change of imidazole moiety upon complexation, Chem. Pharm. Bull., 38, 3140, 10.1248/cpb.38.3140 Udechukwu, 2016, Prospects of enhancing dietary zinc bioavailability with food-derived zinc-chelating peptides, Food Funct., 7, 4137, 10.1039/C6FO00706F