Cited by 227

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

Rationally Designed Peptides and Peptidomimetics as Inhibitors of Amyloid-β (Aβ) Aggregation: Potential Therapeutics of Alzheimer’s Disease

Goyal, Deepti, Shuaib, Suniba, Mann, Sukhmani, Goyal, Bhupesh·2017·ACS Combinatorial Science

Open this paper in CoChat — free account

Abstract

Alzheimer's disease (AD) is a progressive neurodegenerative disease with no clinically accepted treatment to cure or halt its progression. The worldwide effort to develop peptide-based inhibitors of amyloid-β (Aβ) aggregation can be considered an unplanned combinatorial experiment. An understanding of what has been done and achieved may advance our understanding of AD pathology and the discovery of effective therapeutic agents. We review here the history of such peptide-based inhibitors, including those based on the Aβ sequence and those not derived from that sequence, containing both natural and unnatural amino acid building blocks. Peptide-based aggregation inhibitors hold significant promise for future AD therapy owing to their high selectivity, effectiveness, low toxicity, good tolerance, low accumulation in tissues, high chemical and biological diversity, possibility of rational design, and highly developed methods for analyzing their mode of action, proteolytic stability (modified peptides), and blood-brain barrier (BBB) permeability.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1021/acscombsci.6b00116

Cites

23 of 23 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
The global prevalence of dementia: a systematic review and metaanalysis.
Prince, M., Bryce, R., Albanese, E., Wimo, A., Ribeiro, W., & Ferri, C. P. (2013) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2012.11.007 · Cited by 4,941
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo
Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336
The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics
Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188
The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962
Two Phase 3 Trials of Bapineuzumab in Mild-to-Moderate Alzheimer's Disease
Salloway, S., Sperling, R., Fox, N. C., Blennow, K., Klunk, W., Raskind, M., Sabbagh, M., Honig, L. S., Porsteinsson, A. P., Ferris, S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1304839 · Cited by 1,960
The Protein-Folding Problem, 50 Years On
Dill, K. A., & MacCallum, J. L. (2012) · Science · doi:10.1126/science.1219021 · Cited by 1,699
Phase 3 Trials of Solanezumab for Mild-to-Moderate Alzheimer's Disease
Doody, R. S., Thomas, R. G., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., Raman, R., Sun, X., Aisen, P. S., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1312889 · Cited by 1,668
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
A Phase 3 Trial of Semagacestat for Treatment of Alzheimer's Disease
Doody, R. S., Raman, R., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., He, F., Sun, X., Thomas, R. G., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1210951 · Cited by 1,224
Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial
Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988
Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand
Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R., Thyberg, J., Terenius, L., & Nordstedt, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8545 · Cited by 963
Characteristics of Compounds that Cross the Blood-Brain Barrier
Banks, W. A. (2009) · BMC Neurology · doi:10.1186/1471-2377-9-s1-s3 · Cited by 710
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
Effect of Tarenflurbil on Cognitive Decline and Activities of Daily Living in Patients With Mild Alzheimer Disease<subtitle>A Randomized Controlled Trial</subtitle>
Green, R. C. (2009) · JAMA · doi:10.1001/jama.2009.1866 · Cited by 643
REVIEW: Curcumin and Alzheimer’s disease
Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450
Flavonoids, cognition, and dementia: Actions, mechanisms, and potential therapeutic utility for Alzheimer disease
Williams, R. J., & Spencer, J. P. E. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.010 · Cited by 448
β-Amyloid Monomers Are Neuroprotective
Giuffrida, M. L., Caraci, F., Pignataro, B., Cataldo, S., De Bona, P., Bruno, V., Molinaro, G., Pappalardo, G., Messina, A., Palmigiano, A., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.1736-09.2009 · Cited by 421
Davunetide in patients with progressive supranuclear palsy: a randomised, double-blind, placebo-controlled phase 2/3 trial
Boxer, A. L., Lang, A. E., Grossman, M., Knopman, D. S., Miller, B. L., Schneider, L. S., Doody, R. S., Lees, A., Golbe, L. I., Williams, D. R., et al. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70088-2 · Cited by 294
The Potent BACE1 Inhibitor LY2886721 Elicits Robust Central Aβ Pharmacodynamic Responses in Mice, Dogs, and Humans
May, P. C., Willis, B. A., Lowe, S. L., Dean, R. A., Monk, S. A., Cocke, P. J., Audia, J. E., Boggs, L. N., Borders, A. R., Brier, R. A., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.4129-14.2015 · Cited by 206
Aβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease
Gao, C. M., Yam, A. Y., Wang, X., Magdangal, E., Salisbury, C., Peretz, D., Zuckermann, R. N., Connolly, M. D., Hansson, O., Minthon, L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015725 · Cited by 105

Research works printed but not linked: 247

Alzheimer A., 1907, Allg. Zschr. Psychiat. Psych. gerichtl. Med., 64, 146
Hippius H., 2003, Dialogues Clin. Neurosci., 5, 101, 10.31887/DCNS.2003.5.1/hhippius · DOI · Paper page
10.1007/978-94-007-5416-4_14 · DOI · Paper page
10.1016/j.jalz.2016.07.150 · DOI · Paper page
10.1016/j.jalz.2010.01.010 · DOI · Paper page
10.1016/j.jalz.2007.04.381 · DOI · Paper page
10.1146/annurev.publhealth.23.100901.140525 · DOI · Paper page
10.1126/science.275.5300.630 · DOI · Paper page
Selkoe D. J., 2001, Physiol. Rev., 81, 741, 10.1152/physrev.2001.81.2.741 · DOI · Paper page
10.1002/syn.20957 · DOI
10.1001/jamaneurol.2016.0301 · DOI
10.1016/0896-6273(89)90210-9 · DOI · Paper page
10.2353/ajpath.2007.070345 · DOI · Paper page
10.1111/j.1471-4159.2007.04809.x · DOI
10.1021/cr3000994 · DOI · Paper page
10.1016/S0076-6879(99)09015-1 · DOI · Paper page
10.1159/000100355 · DOI · Paper page
10.1021/bi0011330 · DOI · Paper page
10.1002/jnr.10859 · DOI · Paper page
10.1021/bi00172a009 · DOI
10.1016/j.cell.2012.02.022 · DOI · Paper page
10.1186/1750-1326-4-48 · DOI · Paper page
10.1126/science.1213151 · DOI · Paper page
10.1021/acs.jpclett.5b00055 · DOI
10.1080/07391102.2016.1199972 · DOI
10.1039/C6RA10934A · DOI
10.1073/pnas.1411798111 · DOI · Paper page
10.1016/j.biochi.2014.12.007 · DOI · Paper page
10.1002/slct.201600078 · DOI
10.1039/C5RA19015K · DOI
10.1021/jp200743w · DOI
10.1021/jp1062572 · DOI
10.1021/acs.jpcb.5b09678 · DOI
10.1016/j.bpc.2016.03.001 · DOI
10.1016/j.bpc.2010.05.001 · doi:10.1016/j.bpc.2010.05.001
10.1098/rsif.2015.0876 · DOI
10.1080/07391102.2012.703062 · DOI
10.1021/acs.jpcb.6b09216 · DOI
10.1002/psc.2789 · DOI · Paper page
10.1590/S1807-59322011001300006 · DOI · Paper page
10.1021/ja054041c · DOI · Paper page
10.1016/j.bbrc.2005.10.006 · DOI
10.1111/j.1471-4159.2005.03576.x · DOI
10.1038/85525 · DOI · Paper page
10.1016/j.jmb.2011.12.062 · DOI · Paper page
10.1038/nature03659 · DOI · Paper page
10.1073/pnas.0408007101 · DOI
10.1038/nrd2896 · DOI · Paper page
10.1038/nrd2676 · DOI
10.3389/fnagi.2014.00165 · DOI
10.1016/B978-0-12-394816-8.00004-0 · DOI
10.2174/157488911795933938 · DOI
Vincent B., 2011, J. Alzheimers Dis., 24, 75, 10.3233/JAD-2011-110218 · DOI
10.1001/archneurol.2012.2194 · DOI · Paper page
10.1016/j.jalz.2013.05.569 · DOI
10.1038/nn.2433 · DOI · Paper page
10.1039/C4RA09193K · DOI
10.1021/cr300009x · DOI · Paper page
10.1016/S1474-4422(08)70167-4 · DOI · Paper page
10.1159/000358875 · DOI
10.1111/j.1476-5381.2011.01713.x · DOI
10.2174/156720511796717122 · DOI
10.1073/pnas.1208797109 · DOI
10.1212/WNL.0000000000001877 · DOI · Paper page
10.2174/13816128113199990068 · DOI
10.2174/156802607779318262 · DOI · Paper page
10.2174/092986712802430018 · doi:10.2174/092986712802430018
10.1016/j.expneurol.2009.08.032 · DOI
10.1002/cmdc.201500215 · DOI
10.1038/nbt1273 · DOI · Paper page
10.1016/j.jmgm.2005.08.002 · DOI
10.1038/nature06526 · DOI · Paper page
10.1007/s11030-006-9035-3 · DOI
10.1126/science.1101262 · DOI · Paper page
10.1073/pnas.0705888104 · DOI
10.1038/nm790 · DOI · Paper page
10.1126/science.1151839 · DOI · Paper page
10.1073/pnas.1600749113 · DOI · Paper page
10.1073/pnas.262663499 · DOI · Paper page
10.1110/ps.041292205 · DOI · Paper page
10.1371/journal.pone.0090385 · DOI
10.1016/j.sbi.2014.12.004 · DOI · Paper page
10.1038/aps.2011.14 · DOI · Paper page
10.1517/13543776.2013.772983 · DOI
10.2174/092986711797200435 · DOI
10.1021/co5001234 · doi:10.1021/co5001234
10.1016/j.neurobiolaging.2006.02.015 · DOI · Paper page
10.1006/jmbi.1998.1677 · DOI
10.2174/138955751513150923101841 · doi:10.2174/138955751513150923101841
10.1074/jbc.M508246200 · DOI · Paper page
10.1155/2014/350516 · DOI
10.1021/jo4020722 · DOI
10.1021/ar020147q · doi:10.1021/ar020147q
10.1021/ol902131n · DOI
10.1039/c3ra44318c · doi:10.1039/c3ra44318c
10.1002/ejoc.201101744 · doi:10.1002/ejoc.201101744
10.1039/C5CS00889A · DOI · Paper page
10.1038/nchem.2476 · DOI · Paper page
10.2174/0929867323666160909155222 · DOI
10.1016/j.drudis.2014.10.003 · DOI · Paper page
10.2174/138161212799277752 · DOI
10.4161/pri.28220 · DOI
10.1016/j.bmc.2015.02.041 · DOI
10.2174/138955712800493942 · DOI
10.1074/jbc.M211976200 · DOI · Paper page
10.2174/1874070701105010039 · DOI
10.1021/ar8000475 · DOI · Paper page
Doig A. J., 2007, Curr. Opin. Drug Discovery Devel., 10, 533
10.1002/ddr.10074 · DOI
10.1021/acschemneuro.6b00154 · DOI
10.1074/jbc.272.19.12601 · DOI · Paper page
10.1016/j.regpep.2004.03.013 · DOI
10.1006/bbrc.1996.1413 · DOI · Paper page
10.1038/nm0798-822 · DOI · Paper page
10.1096/fj.01-0841fje · DOI · Paper page
10.1038/sj.mp.4001516 · DOI
10.1007/0-387-23226-5_18 · DOI
10.1016/j.nbd.2004.08.007 · DOI
Granic I., 2010, J. Alzheimers Dis., 19, 991, 10.3233/JAD-2010-1297 · DOI
10.1074/jbc.M113.537472 · DOI
10.1021/bi002734u · DOI · Paper page
10.1021/bi982119e · DOI · Paper page
10.1016/S1074-5521(03)00022-X · DOI
10.1021/bi701415b · DOI · Paper page
10.1021/bm401795e · DOI
10.1021/bi982824n · DOI · Paper page
10.3109/13506120108993819 · DOI
10.1002/(SICI)1097-4695(19990605)39:3<371::AID-NEU4>3.3.CO;2-5 · doi:10.1002/(sici)1097-4695(19990605)39:3<371::aid-neu4>3.3.co;2-5
10.1046/j.1471-4159.1996.66041599.x · DOI
10.1021/bi002416v · DOI · Paper page
10.1034/j.1399-3011.2002.11002.x · DOI · Paper page
10.1111/j.1399-3011.2004.00156.x · DOI
10.1002/cmdc.200900191 · DOI
10.2174/1568026024607508 · DOI
10.1074/jbc.M212694200 · DOI
10.1007/s00044-012-0386-2 · DOI
10.1021/bc025526i · DOI
10.1006/bbrc.2001.6191 · DOI
10.1034/j.1399-3011.2003.21028.x · DOI
10.1021/bi0259857 · DOI
10.1021/bi050225s · DOI
10.1074/jbc.M305466200 · DOI
10.1021/bi060837s · DOI · Paper page
10.1021/bi300415v · DOI
http://adisinsight.springer.com/drugs/800027384.
10.1021/ja0600678 · DOI
10.1002/cbic.200700338 · DOI
10.1002/bip.21151 · DOI
10.1021/bc900281b · DOI
10.1016/j.ejmech.2008.03.036 · DOI
10.1111/j.1747-0285.2011.01259.x · DOI
10.1016/j.bbrc.2009.01.090 · DOI
10.1021/cn900019r · DOI
10.1002/psc.1109 · DOI
10.1002/cbic.201600243 · DOI
10.1006/jmbi.2000.3711 · DOI · Paper page
10.1039/c3mb70235a · DOI
10.1016/j.peptides.2010.06.033 · DOI
10.1021/bi100144m · DOI · Paper page
10.1371/journal.pone.0054769 · DOI
10.1016/j.nano.2016.10.006 · DOI
10.1016/j.bmc.2010.06.087 · DOI
10.1016/j.bmcl.2011.07.111 · DOI
10.1016/j.ab.2012.11.025 · DOI
10.1039/C3TB21483D · DOI
10.1002/anie.201405109 · DOI
10.1002/cbic.201402430 · DOI
10.1016/j.bmcl.2015.05.027 · DOI
10.1002/psc.2784 · DOI
10.1038/srep08139 · DOI
10.1021/acschemneuro.6b00175 · DOI
10.1021/acsami.5b00915 · DOI · Paper page
10.1002/chem.201404562 · DOI · Paper page
10.1002/smll.201202612 · DOI
10.1046/j.1471-4159.1995.64010253.x · DOI · Paper page
Pike C. J., 1993, J. Neurosci., 13, 1676, 10.1523/JNEUROSCI.13-04-01676.1993 · DOI · Paper page
10.1006/bbrc.2002.6745 · DOI
10.1073/pnas.0807163105 · DOI · Paper page
10.1021/bi902075h · DOI
10.1021/jm200982p · DOI
10.1016/j.npep.2010.03.001 · DOI
10.1016/j.bbrc.2011.02.067 · DOI
10.1021/acschemneuro.6b00006 · DOI
10.1097/00001756-199906030-00013 · doi:10.1097/00001756-199906030-00013
10.1016/j.bbrc.2004.09.024 · DOI
10.1074/jbc.M003554200 · DOI · Paper page
10.1042/bst0300537 · doi:10.1042/bst0300537
10.1039/B312129A · DOI · Paper page
10.1016/j.bmc.2011.01.021 · DOI
10.1016/j.bmc.2013.08.062 · DOI
10.1021/jm901092h · DOI
10.1016/j.peptides.2003.08.005 · DOI
10.1111/j.1527-3458.2005.tb00053.x · DOI
10.1124/jpet.107.130526 · DOI · Paper page
10.1023/B:MCBI.0000049373.15558.b8 · DOI
10.1080/13506120500350762 · DOI
10.1371/journal.pone.0027649 · DOI
10.1371/journal.pone.0068159 · DOI
Herculano B., 2013, J. Alzheimers Dis., 33, 983, 10.3233/JAD-2012-121324 · DOI
10.1371/journal.pone.0017971 · DOI · Paper page

200 of 247 shown

Current Strategies for Brain Drug Delivery
Dong, X. (2018) · Theranostics · doi:10.7150/thno.21254 · Cited by 954
“The physicochemical factors that influence BBB permeability include molecular weight, charge, lipid solubility, surface activity and relative size of the molecule [2].”
Background
Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease
Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820
Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 346
Current Strategies to Enhance Delivery of Drugs across the Blood–Brain Barrier
Teleanu, R. I., Preda, M. D., Niculescu, A.-G., Vladâcenco, O., Radu, C. I., Grumezescu, A. M., & Teleanu, D. M. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14050987 · Cited by 200

See all 227

Authors: Goyal, D., Shuaib, S., Mann, S., & Goyal, B.
Venue: ACS Combinatorial Science
Publisher: American Chemical Society (ACS)
Published: 2017-01-18
Volume: 19
Issue: 2
Pages: 55-80
ISSN: 2156-8944 (ISSN-L)
2156-8952
DOI: 10.1021/acscombsci.6b00116
OpenAlex: W2564069686
Cited by: 227
References: 23
FWCI: 15.62
Type: journal article
Language: en
Open access: closed
Funders: Science and Engineering Research Board (SB/FT/CS-013/2014, SERB/F/4167/2015-16)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Rationally Designed Peptides and Peptidomimetics as Inhibitors of Amyloid-β (Aβ) Aggregation: Potential Therapeutics of Alzheimer’s Disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources