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References with Amyloid Beta Peptides

Amyloid Beta Peptides in Research Amyloid beta (Aβ) peptides are crucial tools in neurodegenerative disease research, particularly in Alzheimer's disease studies. JPT’s high-quality peptides support researchers in exploring disease mechanisms, identifying biom

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Amyloid Beta Peptides in Research

Amyloid beta (Aβ) peptides are crucial tools in neurodegenerative disease research, particularly in Alzheimer's disease studies. JPT’s high-quality peptides support researchers in exploring disease mechanisms, identifying biomarkers, and developing therapeutic strategies. Below, you will find key studies referencing JPT’s amyloid beta peptides in recent research.

References with Amyloid Beta Peptides

2025

Aβ-reactive T cell polyfunctionality response as a new biomarker for mild cognitive impairmentChio et al., Diagnosis, Assessment & Disease Monitoring (2025) Product used: A21G-Beta-Amyloid (1-42) HFIP treated, PepMix™ Human CMV (pp65)

The structure of amyloid-β (1–42) oligomers in membranemimetic environmentsKuryshev et al., Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy (2025) Product used: Amyloid Beta, V18*Aβ42

Molecular interactions, structural effects, and binding affinities between silver ions (Ag+) and amyloid beta (Aβ) peptidesLakela et al., Scientific Reports (2025) - PMID: 39948350

2024

β-amyloid monomer scavenging by an anticalin protein prevents neuronal hyperactivity in mouse models of Alzheimer’s DiseaseZott et al., Nature Communications (2024) - PMID: 38987287

Novel 6-hydroxybenzothiazol-2-carboxamides as potent and selective monoamine oxidase B inhibitors endowed with neuroprotective activityAl-Saad et al., European Journal of Medicinal Chemistry (2024) - PMID: 38490063

Archive

Residue‑specifc binding of Ni(II) ions infuences the structure and aggregation of amyloid beta (Aβ) peptidesBerntsson et al., Scientific Reports (2023) - PMID: 36849796

β-amyloid monomer scavenging by an anticalin protein prevents neuronal hyperactivityZott et al., Research Square (2023)

Isotope-labeled amyloid-bdoes not transmit to thebrain in a prion-like manner after peripheraladministrationBrackhan et al., EMBO Reports (2022)

A Highly Specific Assay for the Detection of SARS-CoV-2–Reactive CD4+ and CD8+ T Cells in COVID-19 PatientsZelba et al., J Immunology, (2021)

Citrullination of Amyloid-β Peptides in Alzheimer’s DiseaseSoumya Mukherjee et al., ACS Chem Neurosci., (2021)

SARS-CoV-2 Protein Subunit Vaccination of Mice and Rhesus Macaques Elicits Potent and Durable Neutralizing Antibody ResponsesMandolesi et al., Cell Rep Med, (2021)

Single Prime hAd5 Spike (S) + Nucleocapsid (N) Dual Antigen Vaccination of Healthy Volunteers Induces a Ten-Fold Increase in Mean S- and N- T-Cell Responses Equivalent to T-Cell Responses from Patients Previously Infected with SARS-CoV-2Sieling et al., medRxiv, (2021)

Long‑term cafeine treatment of Alzheimer mouse models ameliorates behavioural defcits and neuron loss and promotes cellular and molecular markers of neurogenesisStazi et al., Cellular and Molecular Life Science, (2021)

Population Imaging of Synaptically Released Glutamate in Mouse Hippocampal SlicesUnger et al., STAR Protocols, (2021)

A Rapid and Reliable Liquid Chromatography/mass Spectrometry Method for SARS-CoV-2 Analysis from Gargle Solutions and SalivaKipping et al., Analytic & Bioanalytic Chem., (2021)

COVID-19 Subunit Vaccine with a Combination of TLR1/2 and TLR3 Agonists Induces Robust and Protective ImmunitySoo-Kyung Jeong et al., Vaccine, (2021)

JNJ-64794964 (AL-034/TQ-A3334), a TLR7 Agonist, Induces Sustained Anti-HBV Activity in AAV/HBV Mice Via Non-Cytolytic MechanismsHerschke et al., Antiviral Res (2021)

R1441G but not G2019S Mutation Enhances LRRK2 Mediated Rab10 Phosphorylation in Human Peripheral Blood NeutrophilsYing Fan et al., Acta Neuropathol. (2021)

Sulfated Lactosyl Archaeol Archaeosomes Synergize with Poly(I:C) to Enhance the Immunogenicity and Efficacy of a Synthetic Long Peptide-Based Vaccine in a Melanoma Tumor ModelAkache et al., Pharmaceutical Research, (2021

A Comparative Study of the Effects of Aducanumab and Scanning Ultrasound on Amyloid Plaques and Behavior in the APP23 Mouse Model of Alzheimer DiseaseLeinenga et al., bioRxiv (2020) - PMID: n.a.

Lithium Ions Display Weak Interaction With Amyloid-Beta (Aβ) Peptides And Have Minor Effects On Their AggregationBerntsson et al., BioRxiv (2020) - PMID: n.a.

Analyzing Microglial‑Associated Aβ in Alzheimer’s Disease Transgenic Mice With a Novel Mid‑Domain Aβ‑AntibodyHenjum et al., Scientific Reports (2020) - PMID: 32601313

In Situ Structural Characterization of Early Amyloid Aggregates in Alzheimer’s Disease Transgenic Mice And Octodon DegusBenseny-Cases et al., Scientific Reports (2020) - PMID: 32246090

Metal- and UV- catalyzed oxidation results in trapped amyloid-ß intermediates revealing that self-assembly is required for Aß-induced cytotoxicityMaina et al., iScience (2020) -

Misfolded Amyloid-β-42 Impairs The Endosomal–Lysosomal PathwayMarshall et al., Cellular and Molecular Life Sciences (2020) - PMID: 32025743

Method For Detecting Aggregate Of Aggregate - Forming Polypeptidemethod For Detecting Aggregate Of Aggregate - Forming PolypeptideByoung Sub LEE et al., Patent Application Publication (2019) - PMID: n.a.

Novel D - Enantiomeric Peptides Derived From D3 And Use ThereofWillbold et al., Patent Application Publication (2019) - PMID: n.a.

Poly(propylene imine) Dendrimers With Histidine-Maltose Shell as Novel Type of Nanoparticles for Synapse and Memory ProtectionAso et al., Nanomedicine: Nanotechnology, Biology and Medicine (2019) - PMID: 30708052

The Metalloprotease ADAMTS4 Generates N-truncated Aβ4–x Species and Marks Oligodendrocytes as a Source of Amyloidogenic Peptides in Alzheimer’s DiseaseWalter et al., Acta Neuropathologica (2018) - PMID: 30426203

Amyloid-Peptide β 42 Enhances the Oligomerization and Neurotoxicity of apoE4: The C-Terminal Residues Leu279, Lys282 and Gln284 Modulate the Structural and Functional Properties of apoE4.Dafnis et al., Neuroscience (2018) - PMID: 30367942

A Peptide or Collection of Peptides Derived from Amyloid Precursor ProteinWillem et al., US Patent App. 15/559,613, 2018 (2018) - PMID: n.a.

Synchrotron-Based µFTIR Study on the Effect of Alzheimer´s Aβ Amorphous and Fibrillar Aggregates on PC12 CellsBenseny-Cases et al., Analytical Chemistry (2018) - PMID: 29359921

High Affinity Binding of Monomeric, but not Oligomeric Amyloid-β to Ganglioside GM1 Containing NanodiscsThomaier et al., Biochemistry (2016) - PMID: n.a.

Limited Effects of Prolonged Environmental Enrichment on the Pathology of 5XFAD MiceHüttenrauch et al., Molecular Neurobiology (2016) - PMID: 27734334

A Critical Role For the Self-Assembly of Amyloid-β1-42 in NeurodegenerationMarshall et al., Scientific reports (2016) - PMID: 27443509

Characterization of Insulin-Degrading Enzyme-Mediated Cleavage of Aβ in Distinct Aggregation StatesHubin et al., Biochim Biophys Acta. (2016) - PMID: 26968463

Competitive Mirror Image Phage Display Derived Peptide Modulates Amyloid Beta Aggregation and ToxicityRudolph et al., PLoS One. (2016) - PMID: 26840229

Assessment of Structural Properties of Amyloid Aggregates and Their Application PotentialThangaraj et al., Dissertation for the University of Ulm (2016) - PMID: n.a.

Inhibition of the Cardiac Na+ Channel α-Subunit Nav1. 5 by Propofol and DexmedetomidineStoetzer et al., Naunyn Schmiedebergs Arch Pharmacol. - PMID: 26667357

Aβ-42 Lowering Agents From the Marine-Derived Fungus Dichotomomyces CejpiiHarms et al., Steroids. (2015) - PMID: 26440473

η-Secretase Processing of APP Inhibits Neuronal Activity in the HippocampusWillem et al., Nature (2015) - PMID: 26322584

Hybridization of an Aβ-Specific Antibody Fragment with Aminopyrazole-Based β Sheet Ligands Displays Striking Enhancement of Target AffinityHellmert et al., Org. Biomol. Chem. (2015) - PMID: n.a.

Neprilysin Deficiency Alters the Neuropathological and Behavioral Phenotype in the 5XFAD Mouse Model of Alzheimer's DiseaseHuettenrauch et al., J Alzheimers Dis. (2014) - PMID: 25408216

Monoclonal Antibodies Against Ab42 Fibrils Distinguish Multiple Aggregation State Polymorphisms in vitro and in Alzheimer's Disease BrainHatami et al., J. Biol. Chem. (2014) - PMID: 25281743

The Alzheimer Disease Protective Mutation A2T Modulates Kinetic and Thermodynamic Properties of Amyloid-β (Aβ) AggregationBenilova et al., J. Biol. Chem. (2014) - PMID: 25253695

Structure and Biomedical Applications of Amyloid Oligomer NanoparticlesKumar et al., ACS nano (2014) - PMID: 25337989

Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4Argyri et al., J. Biol. Chem. (2014) - PMID: 24644280

The D-Amino Acid Peptide D3 Reduces Amyloid Fibril Boosted HIV-1 InfectivityWidera et al., AIDS Res. Ther. (2014) - PMID: 24422713

Characterization of a Single-Chain Variable Fragment Recognizing a Linear Epitope of Aβ: A Biotechnical Tool for Studies on Alzheimer’s Disease?Dornieden et al., PLoS One (2013) - PMID: 23555792

Effect of Poly(propylene imine) Glycodendrimers on β-Amyloid Aggregation in Vitro and in APP/PS1 Transgenic Mice, as a Model of Brain Amyloid Deposition and Alzheimer’s DiseaseKlementieva et al., Biomacromolecules (2013) - PMID: 24004423

Nanoparticulate Flurbiprofen Reduces Amyloid-β42 Generation in an in Vitro Blood-Brain Barrier ModelMeister et al., Alzheimers Research & Therapy (2013) - PMID: 24280275

The Amyloid-β Oligomer Count in Cerebrospinal Fluid is a Biomarker for Alzheimer's DiseaseWang-Dietrich et al., Journal of Alzheimer's Disease (2013) - PMID: 23313925

Exploring the Sequence–Structure Relationship for Amyloid PeptidesMorris et al., Biochem. J. (2013) - PMID: 23252554

Analysis of Quality, Aggregation and Toxicity of Amyloid Beta Peptide Produced by JPTVandersteen et al., Report (2011)

Active Immunization with Amyloid-β 1–42 Impairs Memory Performance through TLR2/4-Dependent Activation of the Innate Immune SystemVollmar et al., J. Immunol. (2010) - PMID: 20943998

Mechanism of Amyloid Plaque Formation Suggests an Intracellular Basis of Aβ PathogenicityFriedrich et al., PNAS (2010) - PMID: 20133839

Novel Mediators of Amyloid Precursor Protein SignalingSwistowski et al., J. Neurosci. (2009) - PMID: 20016085

DNA Beta-Amyloid1-42 Trimer Immunization for Alzheimer Disease in a Wild-Type Mouse ModelLambracht-Washington et al., JAMA, (2009) - PMID: 19861672

Vaccination with Prion Peptide-Displaying Papillomavirus-like Particles Induces Autoantibodies to Normal Prion Protein that Interfere with Pathologic Prion Protein Production in Infected CellsHandisurya et al., FEBS Journal (2007) - PMID: 17313482

In Vitro Characterization of Conditions for Amyloid-β Peptide Oligomerization and FibrillogenesisStine et al., J Biol Chem. (2003) - PMID: 12499373

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Related questions

01What Drives MK-6240 Performance?

The performance of MK-6240 appears to be driven largely by differences in biologic binding characteristics, said Pascoal, who is also a behavioral neurologist at the University of Pittsburgh School of Medicine. “The main driver is biological affinity: MK-6240 binds tau tangles with roughly sixfold higher affinity than flortaucipir, as demonstrated in post-mortem tissue,” he explained. “This translates into a stronger signal-to-noise ratio in vivo, allowing detection of the sparse, early tangle deposits in medial temporal regions that flortaucipir tends to miss.” However, access to this newer tau PET tracer remains limited, he acknowledged. “Availability remains a real barrier,” Pascoal said. “MK-6240 is currently produced at a limited number of academic and trial-affiliated PET centers and is not yet approved as a routine clinical test.” The new agent received FDA Fast Track designation in 2025. The agency is expected to issue a decision on the manufacturer Lantheus’ new drug application expected in August, the company reported in a statement . The study provides evidence supporting sensitive approaches to tau detection, said Stephen Salloway, MD, director of Neurology and the Memory and Aging Program at Butler Hospital in Providence, Rhode Island, who was not part of the research. “Early detection of AD pathology will be critical for testing new interventions to slow or prevent cognitive decline in individuals at risk for AD,” and MK-6240 is better at detecting early stages of tau pathology than the currently available tracer, Salloway told Medscape Medical News . However, he cautioned that broader clinical implementation will require additional work to standardize interpretation and staging. “Better molecular staging of AD is needed to improve diagnostic accuracy and to identify individuals most likely to benefit from treatment,” he said. “Nuclear medicine specialists, radiologists, and dementia experts need experience and training to interpret tau PET scans.” The study was funded by the National Institute on Aging. Disclosure information for study authors is available in the original study publication. Salloway reported having no relevant financial disclosures.

Source: www.medscape.com ↗
Research context

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Research areas and applications of Beta-Amyloid (1-42), CAS: 107761-42-2

Neurodegeneration and Alzheimer’s research: Used to study how Amyloid beta 1-42 overproduction, impaired clearance, and rapid aggregation drive Alzheimer’s progression due to its high neurotoxicity and strong synaptic impact. Amyloid aggregation and plaque formation studies: Serves as a model for fast β-sheet nucleation, toxic oligomer formation, and the development of protofibrils and mature fibrils using NMR, AFM, and cryo-EM. Neurotoxicity, synaptic physiology, and neuronal function: Used to examine how beta amyloid oligomers disrupt synaptic signaling, alter calcium balance, impair plasticity, induce oxidative stress, and activate apoptosis that contributes to neuronal dysfunction. Anti-amyloid drug discovery and therapeutic development: Utilized to screen aggregation inhibitors, test Aβ-targeting monoclonal antibodies (e.g., beta amyloid 1-42 antibody), evaluate peptide-based therapeutics, and model compound effects that reduce amyloid burden. Biomarker development and diagnostics: Supports CSF and blood biomarker studies focused on decreased peptide levels and its ratio with Amyloid beta (1-40), both strongly linked to amyloid PET imaging and early Alzheimer’s diagnosis. APP processing and familial Alzheimer’s disease research: Used to analyze how APP, PSEN1, and PSEN2 mutations shift γ-secretase cleavage toward increased Amyloid beta (1-42), modeling mechanisms of familial Alzheimer’s disease. Neuroinflammation research: Applied to study microglial and astrocytic activation, cytokine release, and inflammatory responses induced by Amyloid beta aggregates that stimulate innate immune pathways. Seeding and cross-seeding studies: Used to examine how it acts as a nucleation seed for Aβ (1-40) fibrillization and how mixed Aβ species form distinct fibril structures in plaques. Comparison studies with Aβ (1-40): Used to compare aggregation kinetics, toxicity, structural stability, and diagnostic relevance with Beta amyloid (1-40).

Source: jpt.com ↗

What This Means for Researchers

This convergence of immunology and neuroscience is one of the most exciting fields of study right now. The similarities between LL-37 and Aβ open up entirely new avenues for therapeutic development and a deeper understanding of disease. Could we learn how to control pathological Aβ aggregation by studying how the body successfully regulates LL-37? Could modulating LL-37 levels or its activity be a novel therapeutic strategy for neuroinflammatory diseases? Answering these questions is a formidable challenge. It demands research materials of the highest possible quality. When you're investigating the subtle, concentration-dependent interactions between two peptides that can both help and harm, you simply cannot afford to have impurities or incorrect sequences in your samples. A tiny contaminant could skew aggregation kinetics or trigger an unintended inflammatory response, sending an entire research project down the wrong path. It's a difficult, often moving-target objective. That's the entire reason Real Peptides exists. Our commitment to small-batch synthesis and rigorous quality control ensures that the LL-37 and other compounds researchers use are exactly what they're supposed to be—pure, consistent, and reliable. This level of precision is a non-negotiable element for anyone working on the cutting edge. Our experience shows that breakthroughs are built on a foundation of trustworthy data, which starts with trustworthy reagents. This dedication to quality is something we apply across our full range of peptides. If your lab is ready to explore these complex biological questions, we're here to provide the high-purity tools you need to find clear answers. You can [Get Started Today] and see the difference that uncompromising quality makes. The story of LL-37 and Aβ is a potent reminder that biology doesn't operate in neat silos. The systems that protect us from microbes are deeply intertwined with the processes that can lead to chronic disease and aging. The villain may be a hero in a different context, and the hero's power, left unchecked, can cause its own form of damage. By understanding their surprising similarities, we're not just learning about two peptides; we're gaining a more profound insight into the delicate and often paradoxical nature of life itself.

Source: realpeptides.co ↗
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