The Amyloid-Binding Peptides Research Group Amyloid fibrils are implicated in many disorders including Alzheimer's disease, Parkinson's disease, Type II Diabetes mellitus, Familial British Dementia, Familial Danish Dementia and Creutzfeldt-Jakob disease. The Amyloid-Binding Peptides Research Group has been led by Dr Nat Milton (email: since September 1996 and is based in the School of Clinical & Applied Sciences at Leeds Beckett UniversityThe Amyloid-Binding Peptides Research Group has focused on the identification and characterization of endogenous amyloid-binding compounds. The binding of the Alzheimer's associated amyloid-ß peptide plus amylin and prion protein fragments to human catalase has been characterized by our group (Milton & Harris 2014) and the proposed catalase binding domain of a range of peptides suggested. The mechanisms for catalase neuroprotection against amyloid peptides, including amyloid-ß, amyloid-Bri, amyloid-Dan, amylin and prion protein fragments, have been characterized using an SH-SY5Y cell line overexpressing human catalase (Chilumuri et al 2013). The group has shown that the catalase-amyloid interaction inhibitor benzothiazole aniline-tetra(ethylene glycol) and the catalase activity inhibitor 3-amino-1,2,4-triazole both block catalase neuroprotection leading to enhanced amyloid toxicity in catalase overexpressing neurons. These studies have confirmed that catalase neuroprotection against amyloid peptides involves both an activity dependent component and a catalase-amyloid binding interaction dependent component.

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The group has also identified fibril formation conditions for the non-amyloidogenic rat amylin peptide (Milton & Harris 2013), which have been used to screen for novel amyloid-binding compounds. Using this screening the group has identified a number of amyloid-binding compounds including the R9 peptide, kisspeptin and kissorphins. The kisspeptin binding to the Alzheimer's associated amyloid-ß peptide plus amylin and prion protein fragments has been characterized (Milton et al 2012) and models of KiSS-1 overexpression characterized (Chilumuri & Milton 2013). Other groups have confirmed the utility of both catalase (Nell et al 2016) and kisspeptin (Jiang et al 2015) for prevention of amyloid-ß toxicity in vivo and their potential for therapeutic use in Alzheimer's disease.


The Amyloid-Binding Peptides Research Group discoveries include Amyloid interactions with catalase, kisspeptin peptides plus a phosphorylated derivative of amyloid-ß and cannabinoid neuroprotection against amyloid-ß. The ser26 phosphorylated amyloid-ß has been found in Alzheimer’s disease brains, shows greater toxicity plus less aggregation (Milton 2001Milton 2005) and its presence has been confirmed by others (Kumar et al 2016). The group discovered cannabinoid neuroprotection against amyloid-ß (Milton 2002), which has been confirmed in vivo (Aso & Ferrer 2014) and has potential for development for therapeutic use in Alzheimer's disease. A full list of publications from the Amyloid-Binding Peptides Research Group are included in the Publications page.


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Leeds Beckett University

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