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Note: As of September 30th there will be order processing and shipment delays that may last until October 8, 2020 as we are transitioning to a new ERP system. Please email information@gyrosproteintech.com to discuss what accommodations we can provide during this time.

Unlocking aggregation in amyloid peptides opens up Alzheimer’s research

Sep 30, 2019 9:00:00 AM

Alzheimer's is a progressive degenerative disease of the brain that accounts for 60–80% of dementia cases, which cover a range of cognitive disabilities including memory loss (1). Alzheimer's is the sixth leading cause of death in the United States, with an expected life expectancy of 4–8 years after diagnosis.This disease is not a normal part of aging, and approximately 200,000 Americans under the age of 65 have younger-onset Alzheimer’s disease. There is currently no cure, but symptoms can be treated and great efforts are being made worldwide to improve treatment, delay onset, and ultimately prevent the disease from developing.The amyloid beta peptides involved in Alzheimer’s disease are prone to aggregation, challenging both synthesis and purification. A group based in Auckland New Zealand therefore developed a method to reversibly introduce double linkers into the synthetic peptide that reduce aggregation and improve solubility, resulting in higher yields and purity. 

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Topics: Peptide synthesis, Alzheimer's disease, Tribute peptide synthesizer, SPPS, Amyloid peptides, Pseudoproline

The CWR tripeptide - a promising activator of SIRT1 in the fight against Alzheimer’s disease

Aug 10, 2017 3:00:00 PM

The list of scientific publications by users of our peptide synthesizers is growing steadily.This review article is based on a recent article in the European Journal of Medicinal Chemistry by Rahul Kumar and colleagues at All India Institute of Medical Sciences and School of Computational and Integrative Sciences, Jawaharlal Nehru University in New Delhi, India.

In this study, Rahul Kumar and his colleagues designed and synthesized a novel peptide SIRT1 activator. SIRT1 has been shown to have a protective role against Alzheimer's disease.The peptide, CWR, was tested for its effect on the activity of recombinant SIRT1 protein and also determining its cytotoxicity. CWR was found to be a potent allosteric activator of SIRT1 both by molecular docking and in vitro analysis, increased cell viability and no toxicity to human erythrocytes were also observed.

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Topics: Peptide synthesis, PS3 peptide synthesizer, Alzheimer's disease, SIRT1 activator

Amyloid formation in Alzheimer’s may be modulated by vesicles formed by cholesterol derivatives

Jul 17, 2017 3:59:32 PM

Anomalous protein aggregation has been pinpointed as a prime cause of a number of serious neurodegenerative diseases that include Alzheimer’s, Parkinson’s and Creutzfeldt-Jakob. In the case of Alzheimer’s, protein aggregation starts with cleavage of an amyloid precursor protein (APP) by a secretase to form amyloid-β (Aβ), a family of peptides that form toxic fibrillar plaques, leading to progressive neuron degeneration. This insight has hastened the search for methods to prevent plaque formation. The cholesterol-rich membrane microdomains that promote secretase activity appear to be involved. Added to that, free cholesterol in the cytoplasm can promote the aggregation of Aβ peptides into fibrils, and cholesterol can interact directly with APP and Aβ amyloid fibrils. With this in mind, Elbassal and colleagues at Florida Atlantic University, USA, investigated how cholesterol and its derivatives could affect the formation of fibrils. They showed that the structural properties of the cholesterol-derivative vesicles, including surface charge and vesicle size, are critical in regulating their effect on Aβ40 aggregation kinetics.

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Topics: Peptide synthesis, PS3 peptide synthesizer, Alzheimer's disease, Amyloid formation