NeuroDelta Ltd carry out commercial research using established in silico screening techniques and are headed by their founder and research director Dr Nat Milton.
Dr Milton also leads the Amyloid Binding Peptides Research group, based in the University of Westminster's Faculty of Science & Technology, who conduct academic research in the area of amyloid peptide interactions with proteins.
The Amyloid Binding Peptides Research Group
Amyloid fibrils are implicated in many disorders including Alzheimer's, Parkinson's, Diabetes, Familial British Dementia, Familial Danish Dementia and Creutzfeldt-Jakob Disease. Dr Nat Milton has led research in this area since September 1996 and his Amyloid Binding Peptides research group is currently based in the University of Westminster's Faculty of Science & Technology (Bachem PEPTalk 2013). Dr Milton is also the founder and research director of NeuroDelta Ltd, who carry out commercial research using established in silico screening techniques.
The 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 BTA-EG4 and the catalase activity inhibitor 3-AT 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.
The group has also identified fibril formation conditions for the non-amyloidogenic rat amylin peptide (Milton & Harris 2013), which can be used to screen for novel amyloid-binding compounds. Using this screening we have identified a number of amyloid-binding compounds including the R9 peptide and Kissorphins.
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