Alzheimer's Disease: From Pathology to Therapeutic Approaches

Neuropathological stageing of Alzheimer-related changes.

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Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

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Inflammation and Alzheimer’s disease

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Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B

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Alzheimer's Disease Is a Synaptic Failure

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

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Mild cognitive impairment

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β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

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Opposing Effects of Cucurbit[7]uril and 1,2,3,4,6-Penta-O-galloyl-β- d -glucopyranose on Amyloid β25–35 Assembly

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Resveratrol-maltol hybrids as multi-target-directed agents for Alzheimer’s disease

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DHPC strongly affects the structure and oligomerization propensity of Alzheimer's Aβ(1-40) peptide.

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Synthesis and evaluation of 6-substituted 3-arylcoumarin derivatives as multifunctional acetylcholinesterase/monoamine oxidase B dual inhibitors for the treatment of Alzheimer’s disease

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Rational design of a “sense and treat” system to target amyloid aggregates related to Alzheimer’s disease

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Tuning Structures and Properties for Developing Novel Chemical Tools toward Distinct Pathogenic Elements in Alzheimer’s Disease

Han, J., Lee, H. J., Kim, K. Y., Lee, S. J. C., Suh, J., Cho, J., Chae, J., & Lim, M. H. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00454 · Cited by 29

Novel salicylamide derivatives as potent multifunctional agents for the treatment of Alzheimer's disease: Design, synthesis and biological evaluation

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Modification of Aβ Peptide Aggregation via Covalent Binding of a Series of Ru(III) Complexes

Gomes, L. M., Bataglioli, J. C., Jussila, A. J., Smith, J. R., Walsby, C. J., & Storr, T. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00838 · Cited by 29

Evaluation of N, O-Benzamide difluoroboron derivatives as near-infrared fluorescent probes to detect β-amyloid and tau tangles

Chen, Y., Ouyang, Q., Li, Y., Zeng, Q., Dai, B., Liang, Y., Chen, B., Tan, H., & Cui, M. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113968 · Cited by 29

SAR studies of quinoline and derivatives as potential treatments for Alzheimer’s disease

Li, Z., Yin, L., Zhao, D., Jin, L., Sun, Y.-J., & Tan, C. (2022) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2022.104502 · Cited by 29

Aged dogs demonstrate both increased sensitivity to scopolamine impairment and decreased muscarinic receptor density

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Zn2+ Effect on Structure and Residual Hydrophobicity of Amyloid β-Peptide Monomers

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Neuroprotective effect of 6-paradol enriched ginger extract by fermentation using Schizosaccharomyces pombe

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Synthesis of andrographolide analogues and their neuroprotection and neurite outgrowth-promoting activities

Xu, Y., Wei, H., Wang, J., Wang, W., & Gao, J. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.04.025 · Cited by 29

Real-Time Analysis of Binding Events between Different Aβ1–42 Species and Human Lilrb2 by Dual Polarization Interferometry

Hu, T., Wang, S., Chen, C., Sun, J., & Yang, X. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04950 · Cited by 28

Heterodivalent Linked Macrocyclic β-Sheets with Enhanced Activity against Aβ Aggregation: Two Sites Are Better Than One

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1,2,3,4,6-penta-O-galloyl-β-d-glucopyranose binds to the N-terminal metal binding region to inhibit amyloid β-protein oligomer and fibril formation

de Almeida, N. E. C., Do, T. D., LaPointe, N. E., Jhatro, M., Feinstein, S. C., Shea, J., & Bowers, M. T. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.09.018 · Cited by 30

N-Methyl Mesoporphyrin IX as an Effective Probe for Monitoring Alzheimer’s Disease β-Amyloid Aggregation in Living Cells

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Brain Targeting and Aβ Binding Bifunctional Nanoparticles Inhibit Amyloid Protein Aggregation in APP/PS1 Transgenic Mice

Zhang, X., Zhang, X., Li, Y., Zhong, M., Zhao, P., Guo, C., Xu, H. J., Wang, T., & Gao, H. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00035 · Cited by 29

A near‐infrared probe for detecting and interposing amyloid beta oligomerization in early Alzheimer's disease

Li, Q., Moreno‐González, I., Xie, Z., Gamez, N., Vegas‐Gomez, L., Song, Q., Gu, J., Lin, W., Gomez‐Gutierrez, R., & Wu, T. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12673 · Cited by 28

Novel benzopolycyclic amines with NMDA receptor antagonist activity

Valverde, E., Sureda, F. X., & Vázquez, S. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.03.025 · Cited by 28

Inhibition of Beta‐Amyloid Peptide Aggregation by Multifunctional Carbazole‐Based Fluorophores

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Molecular Lysine Tweezers Counteract Aberrant Protein Aggregation

Hadrović, I., Rebmann, P., Klärner, F., Bitan, G., & Schrader, T. H. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00657 · Cited by 27

N‐(2‐(Piperazin‐1‐yl)phenyl)arylamide Derivatives as β‐Secretase (BACE1) Inhibitors: Simple Synthesis by Ugi Four‐Component Reaction and Biological Evaluation

Edraki, N., Firuzi, O., Fatahi, Y., Mahdavi, M. R., Asadi, M., Emami, S., Divsalar, K., Miri, R., Iraji, A., Khoshneviszadeh, M., et al. (2015) · Archiv der Pharmazie · doi:10.1002/ardp.201400322 · Cited by 27

Dual effects of familial A lzheimer's disease mutations ( D 7 H , D 7 N , and H 6 R ) on amyloid β peptide: Correlation dynamics and zinc binding

Xu, L., Chen, Y., & Wang, X. (2014) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24669 · Cited by 27

Dual Functional Small Molecule Probes as Fluorophore and Ligand for Misfolding Proteins

Zhang, X., & Ran, C. (2013) · Current Organic Chemistry · doi:10.2174/1385272811317060004 · Cited by 26

Enhanced Detection Specificity and Sensitivity of Alzheimer’s Disease Using Amyloid-β-Targeted Quantum Dots

Quan, L. N., Wu, J., Lane, L. A., Wang, J., Lu, Q., Gu, Z., & Wang, Y. (2016) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00019 · Cited by 27

Mitochondrial methionine sulfoxide reductase B2 links oxidative stress to Alzheimer's disease-like pathology

Xiang, X., Li, S., Deng, X., Tang, Y., Min, Z., Luo, B., Wen, Q., Li, K., Chen, J., Ma, Y., et al. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.05.006 · Cited by 26

Single Point Mutation Alters the Microstate Dynamics of Amyloid β-Protein Aβ42 as Revealed by Dihedral Dynamics Analyses

Xu, L., Shan, S., & Wang, X. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp403288b · Cited by 27

Enantiomeric 8-O-4′ type neolignans from red raspberry as potential inhibitors of β-amyloid aggregation

Zhou, L., Lou, L., Wang, W., Lin, B., Chen, J., Wang, X., Huang, X., & Song, S. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.08.007 · Cited by 26

Role of Nanoparticles and Nanomaterials in Drug Delivery: An Overview

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Advances of metallodrug-amyloid β aggregation inhibitors for therapeutic intervention in neurodegenerative diseases: Evaluation of their mechanistic insights and neurotoxicity

Khan, H. Y., Ahmad, A., Hassan, M. N., Khan, Y. H., Arjmand, F., & Khan, R. H. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215580 · Cited by 26

Substrate-Controlled and Organocatalytic Asymmetric Synthesis of Carbocyclic Amino Acid Dipeptide Mimetics

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Importance of the Dimethylamino Functionality on a Multifunctional Framework for Regulating Metals, Amyloid-β, and Oxidative Stress in Alzheimer’s Disease

Derrick, J. S., Kerr, R. A., Korshavn, K. J., McLane, M. J., Kang, J., Nam, E., Ramamoorthy, A., Ruotolo, B. T., & Lim, M. H. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b00525 · Cited by 26

Design, synthesis and evaluation of 2-arylethenyl- N -methylquinolinium derivatives as effective multifunctional agents for Alzheimer's disease treatment

Xia, C., Wang, N., Guo, Q.-L., Liu, Z.-Q., Wu, J., Huang, S., Ou, T., Tan, J., Wang, H., Li, D., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.02.042 · Cited by 26

Two macrocyclic polyamines as modulators of metal-mediated Aβ40aggregation

Yang, Y., Chen, T., Zhu, S., Gu, X., Jia, X., Lu, Y., & Zhu, L. (2015) · Integrative Biology · doi:10.1039/c5ib00064e · Cited by 25

Binding of 12-Crown-4 with Alzheimer’s Aβ40 and Aβ42 Monomers and Its Effect on Their Conformation: Insight from Molecular Dynamics Simulations

Agrawal, N., & Skelton, A. A. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.7b00966 · Cited by 25

Reactivities of cyclam derivatives with metal–amyloid-β

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Neuroprotective Potential and Underlying Pharmacological Mechanism of Carvacrol for Alzheimer’s and Parkinson’s Diseases

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New oxapolycyclic cage amines with NMDA receptor antagonist and trypanocidal activities

Duque, M. D., Camps, P., Torres, E., Valverde, E., Sureda, F. X., López-Querol, M., Camins, A., Prathalingam, S. R., Kelly, J. M., & Vázquez, S. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.11.017 · Cited by 25

Small Molecules and Alzheimer’s Disease: Misfolding, Metabolism and Imaging

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In Situ Monitoring Alzheimer's Disease β‐Amyloid Aggregation and Screening of Aβ Inhibitors Using a Perylene Probe

Li, M., Zhao, C., Yang, X., Ren, J., Xu, C., & Qu, X. (2012) · Small · doi:10.1002/smll.201201543 · Cited by 24

Carbazole-containing arylcarboxamides as BACE1 inhibitors

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Dieta mediterránea y sus efectos benéficos en la prevención de la enfermedad de Alzheimer

Miranda, A., Gómez-Gaete, C., & Sigrid Mennickent, C. (2017) · Revista médica de Chile · doi:10.4067/s0034-98872017000400010 · Cited by 24

Copper(II) complexation of tacrine hybrids with potential anti-neurodegenerative roles

Quintanova, C., Keri, R. S., Chaves, S., & Santos, M. A. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.06.008 · Cited by 23

Copper–amyloid-β complex may catalyze peroxynitrite production in brain: evidence from molecular modeling

Giacovazzi, R., Ciofini, I., Rao, L., Amatore, C. A., & Adamo, C. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp54839b · Cited by 23

Detection of Soluble Amyloid‐β Oligomers and Insoluble High‐Molecular‐Weight Particles in CSF: Development of Methods with Potential for Diagnosis and Therapy Monitoring of Alzheimer′s Disease

Funke, S. A. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/151645 · Cited by 23

Polymethylated acylphloroglucinols from Rhodomyrtus tomentosa exert acetylcholinesterase inhibitory effects

Qin, X., Liu, H., Li, P., Wei Min, N. I., He, L., Khan, A., Hao, X., & Liu, H. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104519 · Cited by 23

Design and synthesis of new theranostic agents for near-infrared imaging of β-amyloid plaques and inhibition of β-amyloid aggregation in Alzheimer's disease

Dao, P., Ye, F., Du, Z. Y., Qian, C., Zhang, K., Dong, C., Meunier, B., & Chen, H. (2017) · Dyes and Pigments · doi:10.1016/j.dyepig.2017.07.071 · Cited by 23

Novel multi target-directed ligands targeting 5-HT4 receptors with in cellulo antioxidant properties as promising leads in Alzheimer's disease

Lanthier, C., Payan, H., Liparulo, I., Hatat, B., Lecoutey, C., Since, M., Davis, A., Bergamini, C., Claeysen, S., Dallemagne, P., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111596 · Cited by 24

Cerebrospinal Fluid Biomarkers in Familial Forms of Alzheimer's Disease and Frontotemporal Dementia

Rostgaard, N., Waldemar, G., Nielsen, J. E., & Simonsen, A. H. (2015) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000381828 · Cited by 23

Amyloid beta(1–42) in aqueous environments: Effects of ionic strength and E22Q (Dutch) mutation

Bossis, F., & Palese, L. L. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.08.010 · Cited by 22

Amyloid Histology Stain for Rapid Bacterial Endospore Imaging

Xia, B., Upadhyayula, S., Nuñez, V., Landsman, P., Lam, S., Malik-Chaudhry, H. K., Gupta, S., Sarshar, M., Hu, J., Anvari, B., et al. (2011) · Journal of Clinical Microbiology · doi:10.1128/jcm.02285-10 · Cited by 22

Graphene oxide-iron oxide nanocomposite as an inhibitor of Aβ 42 amyloid peptide aggregation

Ahmad, I., Mozhi, A., Yang, L., Han, Q., Liang, X., Li, C., Yang, R., & Wang, C. (2017) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2017.08.020 · Cited by 22

Self-Assembly Molecular Chaperone to Concurrently Inhibit the Production and Aggregation of Amyloid β Peptide Associated with Alzheimer’s Disease

Huang, F., Qu, A., Yang, H., Zhu, L., Zhou, H., Liu, J., Long, J., & Shi, L. (2018) · ACS Macro Letters · doi:10.1021/acsmacrolett.8b00495 · Cited by 22

Neuritogenic Militarinone‐Inspired 4‐Hydroxypyridones Target the Stress Pathway Kinase MAP4K4

Schröder, P., Förster, T., Kleine, S., Becker, C. J., Richters, A., Ziegler, S., Rauh, D., Kumar, K., & Waldmann, H. (2015) · Angewandte Chemie · doi:10.1002/ange.201501515 · Cited by 22

Structural optimization of a CXCR2-directed antagonist that indirectly inhibits γ-secretase and reduces Aβ

Bakshi, P., Jin, C., Broutin, P., Berhane, B. T., Reed, J. M., & MULLAN, M. J. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.09.051 · Cited by 22

Recent trends of natural based therapeutics for mitochondria targeting in Alzheimer’s disease

Dhiman, A., Handa, M., Ruwali, M., Singh, D. P., Kesharwani, P., & Shukla, R. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.03.006 · Cited by 21

Effects of Zn2+ Binding on the Structural and Dynamic Properties of Amyloid Β Peptide Associated with Alzheimer’s Disease: Asp1 or Glu11?

Xu, L., Wang, X., & Wang, X. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn4001445 · Cited by 21

Detection of Femtomolar Amyloid-β Peptides for Early-Stage Identification of Alzheimer’s Amyloid-β Aggregation with Functionalized Gold Nanoparticles

Chang, Y., Chien, Y., Chang, C.-C., Wang, P., Chen, Y., & Chang, Y. C. (2024) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c12750 · Cited by 21

Neuroprotective peptide–macrocycle conjugates reveal complex structure–activity relationships in their interactions with amyloid β

Yu, M., Ryan, T. M., Ellis, S., Bush, A. I., Triccas, J. A., Rutledge, P. J., & Todd, M. H. (2014) · Metallomics · doi:10.1039/c4mt00122b · Cited by 20

Self-Assembly of Aβ40, Aβ42 and Aβ43 Peptides in Aqueous Mixtures of Fluorinated Alcohols

Pachahara, S. K., Adicherla, H., & Nagaraj, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0136567 · Cited by 21

A highly sensitive peptide substrate for detecting two Aβ-degrading enzymes: Neprilysin and insulin-degrading enzyme

Chen, P., Liao, T., Hu, C., Wu, S.-T., Wang, S. S. ‐., & Chen, R. P. ‐. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.04.024 · Cited by 21

Peroxynitrite and amyloid-β dual-activated near-infrared theranostic probe for oxidative stress monitoring in Alzheimer's disease

Xue, H., Wang, X., Jiang, Q., Ma, J., & Wong, M. S. (2025) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2025.117201 · Cited by 20

A Peptide-Based Nanocarrier for an Enhanced Delivery and Targeting of Flurbiprofen into the Brain for the Treatment of Alzheimer’s Disease: An In Vitro Study

Al-azzawi, S., Masheta, D., Guildford, A. L., Phillips, G. J., & Santin, M. (2020) · Nanomaterials · doi:10.3390/nano10081590 · Cited by 21

In vivo visualization of enantioselective targeting of amyloid and improvement of cognitive function by clickable chiral metallohelices

Du, Z., Liu, C., Liu, Z., Song, H. L., Scott, P., Du, X., Ren, J., & Qu, X. (2022) · Chemical Science · doi:10.1039/d2sc05897a · Cited by 20

Therapeutic Potential of Active Components from Acorus gramineus and Acorus tatarinowii in Neurological Disorders and Their Application in Korean Medicine

Kim, C. J., Kwak, T. Y., Bae, M. H., Shin, H. K., & Choi, B. T. (2022) · Journal of pharmacopuncture · doi:10.3831/kpi.2022.25.4.326 · Cited by 20

An in situ-triggered and chemi-excited photooxygenation system for Aβ aggregates

Yang, J., Chi, W., Shi, W.-J., Zhang, L., & Yan, J. (2022) · Chemical Engineering Journal · doi:10.1016/j.cej.2022.140998 · Cited by 20

Characterization of the polymorphic states of copper(II)-bound Aβ(1-16) peptides by computational simulations

Xu, L., Wang, X., Shan, S., & Wang, X. (2013) · Journal of Computational Chemistry · doi:10.1002/jcc.23416 · Cited by 20

A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu( ii )

Márquez, M., Blancas‐Mejía, L. M., Campos, A., Rojas-Ochoa, L. F., Castañeda‐Hernández, G., & Quintanar, L. (2014) · Metallomics · doi:10.1039/c4mt00257a · Cited by 20

Molecular crowding effects on the biochemical properties of amyloid β–heme, Aβ–Cu and Aβ–heme–Cu complexes

Li, M. C., Liu, Z., Ren, J., & Qu, X. (2020) · Chemical Science · doi:10.1039/d0sc01020k · Cited by 20

Exploring the role of mitochondrial proteins as molecular target in Alzheimer’s disease

Chadha, S., Behl, T., Sehgal, A., Kumar, A., & BUNGAU, S. G. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.11.008 · Cited by 20

Strategic Design of 2,2′-Bipyridine Derivatives to Modulate Metal–Amyloid-β Aggregation

Ji, Y., Lee, H. J., Kim, M., Nam, G., Lee, S. J. C., Cho, J., Park, C., & Lim, M. H. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b00782 · Cited by 20

Monitoring metal–amyloid-β complexation by a FRET-based probe: design, detection, and inhibitor screening

Lee, H. J., Lee, Y. G., Kang, J., Yang, S. H., Kim, J. H., Ghisaidoobe, A. B. T., Kang, H. J., Lee, S., Lim, M. H., & Chung, S. J. (2018) · Chemical Science · doi:10.1039/c8sc04943b · Cited by 20

Analysis of skeletal diversity of multi-target directed ligands (MTDLs) targeting Alzheimer's disease

Azam, U., Naseer, M. M., & Rochais, C. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117277 · Cited by 22

Bifunctionality of Iminodiacetic Acid-Modified Lysozyme on Inhibiting Zn 2+ -Mediated Amyloid β-Protein Aggregation

Li, X., Xie, B., Dong, X., & Sun, Y. P. (2018) · Langmuir · doi:10.1021/acs.langmuir.8b00254 · Cited by 19

Anti-Alzheimer’s Materials Isolated from Marine Bio-resources: A Review

Rathnayake, A. U., Abuine, R., Kim, Y., & Byun, H. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191024144044 · Cited by 20

Enhancement of the Antioxidant Activity and Neurotherapeutic Features through Pyridol Addition to Tetraazamacrocyclic Molecules

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Donepezil-based hybrids as multifunctional anti-Alzheimer's disease chelating agents: Effect of positional isomerization

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