Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

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Control of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+

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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

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Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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Mutation of the mouse klotho gene leads to a syndrome resembling ageing

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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

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Alzheimer’s disease: Clinical trials and drug development

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Copper in the brain and Alzheimer’s disease

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Molecular Mechanisms of Amyloid Oligomers Toxicity

Kayed, R., & Lasagna‐Reeves, C. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129001 · Cited by 440

Medicinal Inorganic Chemistry Approaches to Passivation and Removal of Aberrant Metal Ions in Disease

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ER stress and UPR in Alzheimer’s disease: mechanisms, pathogenesis, treatments

Ajoolabady, A., Lindholm, D., Ren, J., & Pratico, D. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05153-5 · Cited by 261

Biomarkers of oxidative and nitrosative damage in Alzheimer's disease and mild cognitive impairment

Mangialasche, F., Polidori, M. C., Monastero, R., Ercolani, S., Camarda, C., Cecchetti, R., & Mecocci, P. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.04.002 · Cited by 250

Current and Emerging Drug Treatment Options for Alzheimerʼs Disease

Herrmann, N., Chau, S. A., Kircanski, I., & Lanctôt, K. L. (2011) · Drugs · doi:10.2165/11595870-000000000-00000 · Cited by 245

Up‐regulation of the α‐secretase ADAM10 by retinoic acid receptors and acitretin

Tippmann, F., Hundt, J., Schneider, A., Endres, K., & Fahrenholz, F. (2009) · The FASEB Journal · doi:10.1096/fj.08-121392 · Cited by 231

Lipid-based nanoparticles with high binding affinity for amyloid-β1–42 peptide

Gobbi, M., Re, F., Canovi, M., Beeg, M., Gregori, M., Sesana, S., Sonnino, S., Brogioli, D., Musicanti, C., Gasco, P., et al. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.04.044 · Cited by 192

Neuronal Death Induced by Nanomolar Amyloid β Is Mediated by Primary Phagocytosis of Neurons by Microglia

Neniškytė, U., Neher, J. J., & Brown, G. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.267583 · Cited by 215

Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide

Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202

Overview of Alzheimer’s Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds

Singh, S. K., Srivastav, S., Yadav, A. K., Srikrishna, S., & Perry, G. L. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7361613 · Cited by 196

RAGE and Alzheimer's Disease: A Progression Factor for Amyloid-β-Induced Cellular Perturbation?

Yan, S. D., Bierhaus, A., Nawroth, P. P., & Stern, D. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1030 · Cited by 184

Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 1: An overview

Hureau, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.037 · Cited by 183

The Neurotrophins and Their Role in Alzheimers Disease

Allen, S. J., Watson, J. J., & Dawbarn, D. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376190 · Cited by 184

Cu(II) Affinity for the Alzheimer’s Peptide: Tyrosine Fluorescence Studies Revisited

Aliès, B., Renaglia, E., Rózga, M., Bal, W., Faller, P., & Hureau, C. (2012) · Analytical Chemistry · doi:10.1021/ac302629u · Cited by 172

Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease

Guerrero-Muñoz, M. J., Gerson, J., & Castillo-Carranza, D. L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00464 · Cited by 168

Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 2: Dependence of Cu(II) binding sites with Aβ sequences

Hureau, C., & Dorlet, P. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.034 · Cited by 148

Alzheimer's disease & metals: therapeutic opportunities

Kenche, V. B., & Barnham, K. J. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01221.x · Cited by 147

Herpes simplex virus type I induces the accumulation of intracellular β-amyloid in autophagic compartments and the inhibition of the non-amyloidogenic pathway in human neuroblastoma cells

Santana, S., Recuero, M., Bullido, M. J., Valdivieso, F., & Aldudo, J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.12.010 · Cited by 131

Protective Effects of Fucoidan on Aβ25–35 and d-Gal-Induced Neurotoxicity in PC12 Cells and d-Gal-Induced Cognitive Dysfunction in Mice

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Structural characterization of Cu2+, Ni2+ and Zn2+ binding sites of model peptides associated with neurodegenerative diseases

Migliorini, C., Porciatti, E., Łuczkowski, M., & Valensin, D. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.07.004 · Cited by 117

Fucoidan, a sulfated polysaccharide from brown algae, improves cognitive impairment induced by infusion of Aβ peptide in rats

Gao, Y., Li, C., Yin, J., Shen, J., Wang, H., Wu, Y., & Jin, H. (2011) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2011.12.022 · Cited by 114

Formation of dopamine-mediated α-synuclein-soluble oligomers requires methionine oxidation

Leong, S. L., Pham, C. L. L., Galatis, D., Fodero‐Tavoletti, M. T., Perez, K. A., Hill, A. F., Masters, C. L., Ali, F. E. A., Barnham, K. J., & Cappai, R. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.009 · Cited by 114

Ion Mobility Separation Coupled with MS Detects Two Structural States of Alzheimer's Disease Aβ1–40 Peptide Oligomers

Kłoniecki, M., Jabłonowska, A., Poznański, J. T., Langridge, J., Hughes, C. J., Campuzano, I. D. G., Giles, K., & Dadlez, M. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.01.012 · Cited by 109

Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., & Kayed, R. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.023 · Cited by 105

The induction of HIF‐1 reduces astrocyte activation by amyloid beta peptide

Schubert, D. A., Soucek, T., & Blouw, B. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06712.x · Cited by 90

Development of Bifunctional Stilbene Derivatives for Targeting and Modulating Metal-Amyloid-β Species

Braymer, J. J., Choi, J.-S., DeToma, A. S., Wang, C., Nam, K., Kampf, J. W., Ramamoorthy, A., & Lim, M. H. (2011) · Inorganic Chemistry · doi:10.1021/ic2012205 · Cited by 89

Binding of β-Amyloid (1–42) Peptide to Negatively Charged Phospholipid Membranes in the Liquid-Ordered State: Modeling and Experimental Studies

Ahyayauch, H., Raab, M., Busto, J. V., Andraka, N., Arrondo, J.-L. R., Masserini, M., Tvaroška, I., & Goñi, F. M. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.06.043 · Cited by 88

Modes of Aβ toxicity in Alzheimer’s disease

Götz, J., Eckert, A., Matamales, M., Ittner, L. M., & Liu, X. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0750-2 · Cited by 87

pH-Dependent Cu(II) Coordination to Amyloid-β Peptide: Impact of Sequence Alterations, Including the H6R and D7N Familial Mutations.

Aliès, B., Eury, H., Bijani, C., Rechignat, L., Faller, P., & Hureau, C. (2011) · Inorganic Chemistry · doi:10.1021/ic201739n · Cited by 80

Inhibition of the Mitochondrial Enzyme ABAD Restores the Amyloid-β-Mediated Deregulation of Estradiol

Lim, Y., Grimm, A., Giese, M. H., Mensah‐Nyagan, A. G., Villafranca, J. E., Ittner, L. M., Eckert, A., & Götz, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028887 · Cited by 82

Copper(II) Coordination to Amyloid β: Murine versus Human Peptide

Eury, H., Bijani, C., Faller, P., & Hureau, C. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201005838 · Cited by 79

Protective effects of linalool against amyloid beta-induced cognitive deficits and damages in mice

Xu, P., Wang, K., Lü, C., Dong, L., Gao, L., Yan, M., Aibai, S., Yang, Y., & Liu, X. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.02.010 · Cited by 79

An integrated study of the affinities of the Aβ16 peptide for Cu( i ) and Cu( ii ): implications for the catalytic production of reactive oxygen species

Young, T. R., Kirchner, A., Wedd, A. G., & Xiao, Z. (2014) · Metallomics · doi:10.1039/c4mt00001c · Cited by 74

Blood-Borne Amyloid-β Dimer Correlates with Clinical Markers of Alzheimer's Disease

Villemagne, V. L., Perez, K. A., Pike, K. E., Kok, W. M., Rowe, C. C., White, A. R., Bourgeat, P., Salvado, O., Bedő, J., Hutton, C. A., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5180-09.2010 · Cited by 72

Protective Effects of Baicalin on Aβ1–42-Induced Learning and Memory Deficit, Oxidative Stress, and Apoptosis in Rat

Haitao, D., Wang, H., Zhao, Y., Sun, D., & Xu, Z. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0156-z · Cited by 69

Alzheimer’s Disease and Stem Cell Therapy

Choi, S. S., Lee, S., Kim, S. U., & Lee, H. J. (2014) · Experimental Neurobiology · doi:10.5607/en.2014.23.1.45 · Cited by 62

Adsorption Mechanism and Collapse Propensities of the Full-Length, Monomeric Aβ1-42 on the Surface of a Single-Walled Carbon Nanotube: A Molecular Dynamics Simulation Study

Jana, A. K., & Sengupta, N. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.03.036 · Cited by 59

Protective Effects ofBorago officinalisExtract on Amyloidβ-Peptide(25–35)-Induced Memory Impairment in Male Rats: A Behavioral Study

Ghahremanitamadon, F., Shahidi, ‬., Zargooshnia, S., Nikkhah, A., Ranjbar, A., & Asl, S. S. (2014) · BioMed Research International · doi:10.1155/2014/798535 · Cited by 56

Functional Roles of Amyloid-β Protein Precursor and Amyloid-β Peptides: Evidence from Experimental Studies

Hiltunen, M. O., van Groen, T., & Jolkkonen, J. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1154 · Cited by 62

The neuroprotective effects of β-hydroxybutyrate on Aβ-injected rat hippocampus in vivo and in Aβ-treated PC-12 cells in vitro

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Copper Chelators: Chemical Properties and Bio-medical Applications

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New and emerging treatments for Alzheimer’s disease

Corbett, A., Smith, J. S., & Ballard, C. G. (2012) · Expert Review of Neurotherapeutics · doi:10.1586/ern.12.43 · Cited by 58

The Molecular Assembly of Amyloid Aβ Controls Its Neurotoxicity and Binding to Cellular Proteins

Manzoni, C., Colombo, L., Bigini, P., Diana, V., Cagnotto, A., Messa, M., Lupi, M., Bonetto, V., Pignataro, M., Airoldi, C., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024909 · Cited by 55

A molecular dynamics study of the early stages of amyloid‐β(1–42) oligomerization: The role of lipid membranes

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Stereospecific interactions are necessary for Alzheimer disease amyloid-β toxicity.

Ciccotosto, G., Tew, D., Drew, S., Smith, D. G., Johanssen, T., Lal, V., Lau, T., Perez, K., Curtain, C., Wade, J., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.018 · Cited by 48

Interference of a new cyclometallated Pt compound with Cu binding to amyloid-β peptide

Sasaki, I., Bijani, C., Mallet‐Ladeira, S., Bourdon, V., Faller, P., & Hureau, C. (2012) · Dalton Transactions · doi:10.1039/c2dt12177h · Cited by 50

Lipid raft disarrangement as a result of neuropathological progresses: A novel strategy for early diagnosis?

Marín, R., Rojo, J. A. P., Fabelo, N., Fernandez, C. E., & Díaz, M. L. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.04.025 · Cited by 51

Role of neurotoxicants in the pathogenesis of Alzheimer’s disease: a mechanistic insight

Nisa, F. Y., Rahman, M. A., Hossen, M. A., Khan, M. F., Khan, M. A. N., Majid, M., Sultana, F., & Haque, M. A. (2021) · Annals of Medicine · doi:10.1080/07853890.2021.1966088 · Cited by 44

Transferrin as a drug carrier: Cytotoxicity, cellular uptake and transport kinetics of doxorubicin transferrin conjugate in the human leukemia cells

Szwed, M., Matusiak, A., Laroche‐Clary, A., Robert, J., Marszałek, I., & Jóźwiak, Z. (2013) · Toxicology in Vitro · doi:10.1016/j.tiv.2013.09.013 · Cited by 44

Azo-dyes based small bifunctional molecules for metal chelation and controlling amyloid formation

Rana, M., Cho, H., Roy, T. K., Mirica, L. M., & Sharma, A. K. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.11.029 · Cited by 40

An update on the toxicity of Aβ in Alzheimer’s disease

Götz, J. (2008) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s3016 · Cited by 40

Suppression of Amyloid β A11 Antibody Immunoreactivity by Vitamin C

Cheng, F., Cappai, R., Ciccotosto, G. D., Svensson, G., Multhaup, G., Fransson, L., & Mani, K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243345 · Cited by 39

Structure and Physicochemical Properties of the Aβ42 Tetramer: Multiscale Molecular Dynamics Simulations

Nguyen, H. L., Krupa, P., Hai, N. M., Linh, H. Q., & Li, M. S. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b04208 · Cited by 38

Intracerebroventricular injection of beta-amyloid in mice is associated with long-term cognitive impairment in the modified hole-board test

Schmid, S., Jungwirth, B., Gehlert, V., Blobner, M., Schneider, G. H., Kratzer, S., Kellermann, K., & Rammes, G. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.02.007 · Cited by 34

Roles of zinc ions and structural polymorphism of β-amyloid in the development of Alzheimer’s disease

Kulikova, A. A., Makarov, A. А., & Kozin, S. A. (2015) · Molecular Biology · doi:10.1134/s0026893315020065 · Cited by 35

Critical roles of key domains in complete adsorption of Aβ peptide on single-walled carbon nanotubes: insights with point mutations and MD simulations

Jana, A. K., Jose, J. C., & Sengupta, N. (2012) · Physical Chemistry Chemical Physics · doi:10.1039/c2cp42933k · Cited by 33

Therapeutic efficacy of stemazole in a beta-amyloid injection rat model of Alzheimer's disease

Han, M., Liu, Y. M., Tan, Q., Zhang, B., Wang, W., Liu, J., Zhang, X., Wang, Y., & Zhang, J. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.01.065 · Cited by 33

Cross Dimerization of Amyloid-β and αSynuclein Proteins in Aqueous Environment: A Molecular Dynamics Simulations Study

Jose, J. C., Chatterjee, P., & Sengupta, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106883 · Cited by 32

Metals, Membranes, and Amyloid-β Oligomers: Key Pieces in the Alzheimer's Disease Puzzle?

Watt, A. D., Villemagne, V. L., & Barnham, K. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129017 · Cited by 33

Ion channel activity of brain abundant protein BASP1 in planar lipid bilayers

Ostroumova, O. S., Schagina, L. V., Mosevitsky, M. I., & Zakharov, V. V. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07967.x · Cited by 29

The impact of luteinizing hormone and testosterone on beta amyloid (Aβ) accumulation: Animal and human clinical studies

Verdile, G., Asih, P. R., Barron, A. M., Wahjoepramono, E. J., Ittner, L. M., & Martins, R. N. (2015) · Hormones and Behavior · doi:10.1016/j.yhbeh.2015.05.020 · Cited by 31

Preclinical to phase II amyloid beta (Aβ) peptide modulators under investigation for Alzheimer’s disease

Parsons, C. G., & Rammes, G. (2017) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2017.1313832 · Cited by 29

New and emerging treatments for Alzheimer's disease

Corbett, A., & Ballard, C. G. (2012) · Expert Opinion on Emerging Drugs · doi:10.1517/14728214.2012.675327 · Cited by 27

MRZ-99030 – A novel modulator of Aβ aggregation: II – Reversal of Aβ oligomer-induced deficits in long-term potentiation (LTP) and cognitive performance in rats and mice

Rammes, G., Gravius, A., Ruitenberg, M., Wegener, N., Chambon, C., Sroka, K., Jeggo, R., Staniaszek, L. E., Spanswick, D. C., O‘Hare, E., et al. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.12.037 · Cited by 51

Challenges in Designing Therapeutic Agents for Treating Alzheimer’s Disease-from Serendipity to Rationality

Rashid, U., & Ansari, F. L. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50002-7 · Cited by 23

APP involvement in retinogenesis of mice

Dinet, V., An, N., Ciccotosto, G. D., Bruban, J., Maoui, A., Bellingham, S. A., Hill, A. F., Andersen, O. M., Nykjær, A., Jonet, L., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0762-2 · Cited by 21

Anti-Aβ drug candidates in clinical trials and plasmonic nanoparticle-based drug-screen for Alzheimer's disease

Lee, D., Lee, G., & Yoon, D. S. (2018) · The Analyst · doi:10.1039/c7an02013a · Cited by 20

Protective effect and mechanism of docosahexaenoic acid on the cognitive function in female APP/PS1 mice

Bie, N., Li, J., Li, C., Lian, R., Qin, L., & Wang, C. (2021) · Food & Function · doi:10.1039/d1fo01922h · Cited by 18

Herpes Simplex Virus Type 1 Enhances Expression of the Synaptic Protein Arc for Its Own Benefit

Acuña, F., Muñoz, M., Hott, M., Martín, C., Mancilla, E., Salazar, P., Leyton, L., Zambrano, Á., Concha, M. I., Burgos, P. V., et al. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00505 · Cited by 16

Copper(II) Coordination to Amyloid β: Murine versus Human Peptide

Eury, H., Bijani, C., Faller, P., & Hureau, C. (2010) · Angewandte Chemie · doi:10.1002/ange.201005838 · Cited by 15

[18F]ROStrace detects oxidative stress in vivo and predicts progression of Alzheimer’s disease pathology in APP/PS1 mice

Hsieh, C., Hou, C., Zhu, Y., Lee, J. Y., Kohli, N., Gallagher, E. P., Xu, K., Lee, H. S., Li, S., McManus, M. J., et al. (2022) · EJNMMI Research · doi:10.1186/s13550-022-00914-x · Cited by 16

Amyloid Precursor-Like Protein 2 deletion-induced retinal synaptopathy related to congenital stationary night blindness: structural, functional and molecular characteristics

Dinet, V., Ciccotosto, G. D., Delaunay, K., Borras, C., Ranchon‐Cole, I., Kostic, C., Savoldelli, M., Sanharawi, M. E., Jonet, L., Pirou, C., et al. (2016) · Molecular Brain · doi:10.1186/s13041-016-0245-z · Cited by 12

Molecular dynamics simulation studies of the structural response of an isolated Aβ1–42 monomer localized in the vicinity of the hydrophilic TiO2 surface

Jose, J. C., & Sengupta, N. (2013) · European Biophysics Journal · doi:10.1007/s00249-013-0900-6 · Cited by 10

Surface induced collapse of Aβ1-42 with the F19A replacement following adsorption on a single walled carbon nanotube

Jana, A. K., & Sengupta, N. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.09.008 · Cited by 10

Oligomer Formation and Cross‐Seeding: The New Frontier

Farmer, K. M., Gerson, J. E., & Kayed, R. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600103 · Cited by 10

Alzheimer’s disease: ageing-related or age-related? New hypotheses from an old debate

Bugiani, O. (2011) · Neurological Sciences · doi:10.1007/s10072-011-0614-4 · Cited by 8

Clinical Trials and Drug Development

Mahipal, A. (2014) · Cancer Control · doi:10.1177/107327481402100301 · Cited by 8

Critical analysis of the use of β-site amyloid precursor protein-cleaving enzyme 1 inhibitors in the treatment of Alzheimer's disease

Evin, G. M., & Barakat, A. (2014) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s41056 · Cited by 6

Huprines — an insight into the synthesis and biological properties

Mezeiová, E., Soukup, O., & Korábečný, J. (2020) · Russian Chemical Reviews · doi:10.1070/rcr4938 · Cited by 7

Photodynamic and Photothermal Therapies using Nanotechnology Approach in Alzheimer's Disease

Ozturk, B., Demir, H., Silindir‐Gunay, M., Akdağ, Y., Şahin, S., & Gülsün, T. (2025) · Current Neuropharmacology · doi:10.2174/011570159x370790250317045223 · Cited by 5

Stability of the Aβ42 Peptide in Mixed Solutions of Denaturants and Proline

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