{"id":{"repo_id":"lancaster","oai_identifier":"oai:eprints.lancs.ac.uk:78064"},"canonical_url":"https://search.dev.ndltd.org/etd/lancaster/oai:eprints.lancs.ac.uk:78064","repository":{"repo_id":"lancaster","name":"Lancaster University","base_url":"https://eprints.lancs.ac.uk/cgi/oai2"},"display":{"title":"Recombinant production of Aβ1-42 peptide and analysis of interactions between Aβ1-42 and Peptide Inhibitor NanoParticles (PINPs) developed as a potential novel treatment for Alzheimer’s Disease","abstract":"This study addressed two main aims relating to the Aβ1-42 peptide – widely demonstrated to play a key role in the pathogenesis of Alzheimer’s Disease (AD). Aβ1-42 is an amyloid peptide that readily self-associates forming neurotoxic aggregates. With the primary risk factor for AD being age, and ageing populations increasing, the need for research into methods of reducing the levels of Aβ1-42 aggregates has never been greater. The first aim of this study was to recombinantly produce the Aβ1-42 peptide using a previously published protocol in order to produce stocks for future experimental use. Producing Aβ1-42 recombinantly results in less peptide variability than occurs via peptide synthesis, and is a much cheaper source of the peptide than commercial procurement. The peptide was expressed by induction of Escherichia coli to express a fusion protein encoding the Aβ1-42 peptide in addition to specific regions necessary for purification. Analysis of the purified Aβ1-42 peptide by transmission electron microscopy demonstrated that the peptide was able to self-associate forming a variety of structures characteristic of Aβ1-42 aggregation as illustrated in the literature. The second aim of the study was to evalauate the effect of Peptide Inhibitor NanoParticles (PINPs) upon Aβ1-42 aggregation. PINPs are second-generation liposomes with the RI-OR2- TAT peptide attached to the surface. RI-OR2-TAT has been found previously to reduce Aβ1-42 aggregation in mouse models of AD. Analysis of the effect of PINPs upon Aβ1-42 aggregation 2 was performed using transmission electron microscopy and fluorescence based assays with PINPs being found to directly bind early and late stage Aβ1-42 aggregates and reduce levels of aggregation. Based on the findings of this study, amendments to the Aβ1-42 production protocol are proposed and it is recommended that PINPs be carried forward into clinical trials as a potential treatment option for AD.","abstract_html":"This study addressed two main aims relating to the Aβ1-42 peptide – widely demonstrated to play a key role in the pathogenesis of Alzheimer’s Disease (AD). Aβ1-42 is an amyloid peptide that readily self-associates forming neurotoxic aggregates. With the primary risk factor for AD being age, and ageing populations increasing, the need for research into methods of reducing the levels of Aβ1-42 aggregates has never been greater. The first aim of this study was to recombinantly produce the Aβ1-42 peptide using a previously published protocol in order to produce stocks for future experimental use. Producing Aβ1-42 recombinantly results in less peptide variability than occurs via peptide synthesis, and is a much cheaper source of the peptide than commercial procurement. The peptide was expressed by induction of Escherichia coli to express a fusion protein encoding the Aβ1-42 peptide in addition to specific regions necessary for purification. Analysis of the purified Aβ1-42 peptide by transmission electron microscopy demonstrated that the peptide was able to self-associate forming a variety of structures characteristic of Aβ1-42 aggregation as illustrated in the literature. The second aim of the study was to evalauate the effect of Peptide Inhibitor NanoParticles (PINPs) upon Aβ1-42 aggregation. PINPs are second-generation liposomes with the RI-OR2- TAT peptide attached to the surface. RI-OR2-TAT has been found previously to reduce Aβ1-42 aggregation in mouse models of AD. Analysis of the effect of PINPs upon Aβ1-42 aggregation 2 was performed using transmission electron microscopy and fluorescence based assays with PINPs being found to directly bind early and late stage Aβ1-42 aggregates and reduce levels of aggregation. Based on the findings of this study, amendments to the Aβ1-42 production protocol are proposed and it is recommended that PINPs be carried forward into clinical trials as a potential treatment option for AD.","abstract_has_math":false,"creators":["Sherer, Mike","Allsop, David","Fullwood, Nigel"],"institution":"Lancaster University","degree_name":"masters","degree_level":"masters","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2016,"date_issued":"2016-01","date_published":"2016-01","updated_at":"2026-07-24T02:48:27Z","subjects":[],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Sherer, Mike","Allsop, David","Fullwood, Nigel"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2016-01-29"]},{"key":"dc:date.issued","label":"Date","values":["2016-01"]},{"key":"dc:publisher.commercial","label":"Dc Publisher Commercial","values":["Lancaster University"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Biomedical & Life Sciences"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["Lancaster University"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://eprints.lancs.ac.uk/id/eprint/78064/"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["masters"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["masters"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://eprints.lancs.ac.uk/id/eprint/78064/1/2016sherermsc.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["This study addressed two main aims relating to the Aβ1-42 peptide – widely demonstrated to play a key role in the pathogenesis of Alzheimer’s Disease (AD). Aβ1-42 is an amyloid peptide that readily self-associates forming neurotoxic aggregates. With the primary risk factor for AD being age, and ageing populations increasing, the need for research into methods of reducing the levels of Aβ1-42 aggregates has never been greater. The first aim of this study was to recombinantly produce the Aβ1-42 peptide using a previously published protocol in order to produce stocks for future experimental use. Producing Aβ1-42 recombinantly results in less peptide variability than occurs via peptide synthesis, and is a much cheaper source of the peptide than commercial procurement. The peptide was expressed by induction of Escherichia coli to express a fusion protein encoding the Aβ1-42 peptide in addition to specific regions necessary for purification. Analysis of the purified Aβ1-42 peptide by transmission electron microscopy demonstrated that the peptide was able to self-associate forming a variety of structures characteristic of Aβ1-42 aggregation as illustrated in the literature. The second aim of the study was to evalauate the effect of Peptide Inhibitor NanoParticles (PINPs) upon Aβ1-42 aggregation. PINPs are second-generation liposomes with the RI-OR2- TAT peptide attached to the surface. RI-OR2-TAT has been found previously to reduce Aβ1-42 aggregation in mouse models of AD. Analysis of the effect of PINPs upon Aβ1-42 aggregation 2 was performed using transmission electron microscopy and fluorescence based assays with PINPs being found to directly bind early and late stage Aβ1-42 aggregates and reduce levels of aggregation. Based on the findings of this study, amendments to the Aβ1-42 production protocol are proposed and it is recommended that PINPs be carried forward into clinical trials as a potential treatment option for AD."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Recombinant production of Aβ1-42 peptide and analysis of interactions between Aβ1-42 and Peptide Inhibitor NanoParticles (PINPs) developed as a potential novel treatment for Alzheimer’s Disease"]}]}],"canonical_facts":{"dc:creator":["Sherer, Mike","Allsop, David","Fullwood, Nigel"],"dc:date":["2016-01-29"],"dc:date.issued":["2016-01"],"dc:description.abstract":["This study addressed two main aims relating to the Aβ1-42 peptide – widely demonstrated to play a key role in the pathogenesis of Alzheimer’s Disease (AD). Aβ1-42 is an amyloid peptide that readily self-associates forming neurotoxic aggregates. With the primary risk factor for AD being age, and ageing populations increasing, the need for research into methods of reducing the levels of Aβ1-42 aggregates has never been greater. The first aim of this study was to recombinantly produce the Aβ1-42 peptide using a previously published protocol in order to produce stocks for future experimental use. Producing Aβ1-42 recombinantly results in less peptide variability than occurs via peptide synthesis, and is a much cheaper source of the peptide than commercial procurement. The peptide was expressed by induction of Escherichia coli to express a fusion protein encoding the Aβ1-42 peptide in addition to specific regions necessary for purification. Analysis of the purified Aβ1-42 peptide by transmission electron microscopy demonstrated that the peptide was able to self-associate forming a variety of structures characteristic of Aβ1-42 aggregation as illustrated in the literature. The second aim of the study was to evalauate the effect of Peptide Inhibitor NanoParticles (PINPs) upon Aβ1-42 aggregation. PINPs are second-generation liposomes with the RI-OR2- TAT peptide attached to the surface. RI-OR2-TAT has been found previously to reduce Aβ1-42 aggregation in mouse models of AD. Analysis of the effect of PINPs upon Aβ1-42 aggregation 2 was performed using transmission electron microscopy and fluorescence based assays with PINPs being found to directly bind early and late stage Aβ1-42 aggregates and reduce levels of aggregation. Based on the findings of this study, amendments to the Aβ1-42 production protocol are proposed and it is recommended that PINPs be carried forward into clinical trials as a potential treatment option for AD."],"dc:format":["application/pdf"],"dc:identifier.uri":["https://eprints.lancs.ac.uk/id/eprint/78064/1/2016sherermsc.pdf"],"dc:publisher.commercial":["Lancaster University"],"dc:publisher.department":["Biomedical & Life Sciences"],"dc:publisher.institution":["Lancaster University"],"dc:relation.isreferencedby":["https://eprints.lancs.ac.uk/id/eprint/78064/"],"dc:title":["Recombinant production of Aβ1-42 peptide and analysis of interactions between Aβ1-42 and Peptide Inhibitor NanoParticles (PINPs) developed as a potential novel treatment for Alzheimer’s Disease"],"dc:type":["Thesis"],"dc:type.qualificationlevel":["masters"],"dc:type.qualificationname":["masters"]},"updated_at":"2026-07-24T02:48:27Z"}