The Amyloid-Binding Peptides Research Group 


The Amyloid-Binding Peptides Research Group has been led by Dr Nat Milton since September 1996 and is based in the School of Clinical & Applied Sciences at Leeds Beckett University.  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 group has focused on the identification and characterization of endogenous anti-amyloid compounds.


The Amyloid-Binding Peptides Research Group discoveries include Amyloid peptide interactions with catalase (Chilumuri et al 2013Milton & Harris 2014), kisspeptin peptides (Milton et al 2012) plus a phosphorylated derivative of amyloid-ß (Milton 2001) and cannabinoid neuroprotection against amyloid-ß (Milton 2002). 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 discovery of cannabinoid neuroprotection against amyloid-ß (Milton 2002) has been confirmed in vivo (Aso & Ferrer 2014) and shows potential for development of cannabinoid agonists 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.


We have 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 kissorphin.


The kissorphin peptide is a novel NPFF-like derivative of kisspeptin (Milton 2012; Gibula-Bruzda et al 2017) and shows binding to the Alzheimer's associated amyloid-ß peptide plus amylin and prion protein fragments (Milton et al 2012). Models of KiSS-1 overexpression have been characterized (Chilumuri & Milton 2013) and protect against amyloid toxicity. Other groups have confirmed the utility of kisspeptin (Jiang et al 2015) and catalase (Nell et al 2016) for prevention of amyloid-ß toxicity in vivo and their potential for therapeutic use in Alzheimer's disease. A UK patent application for the use of kissorphin peptides in the treatment of Alzheimer's disease, Creutzfeldt jakob disease and diabetes mellitus (Milton 2013) has now reached the intention to grant phase.


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