Knob Socket Analysis of Beta Amyloid Proteins - CORE CORE Services Services overviewExplore all CORE services Access to raw data API Dataset FastSync Content discovery Recommender Discovery Managing content Repository dashboard Packages Repository edition About About us Our mission Team Blog FAQs Contact us Knob Socket Analysis of Beta Amyloid Proteins Authors Jihee Yoon Irene Lang Publication date April 30, 2016 Publisher Scholarly Commons Abstract Alzheimer\u27s disease is an irreversible brain disorder that gradually destroys memory, critical thinking skills, and the ability to carry out simple tasks. Currently, this disease affects 5.2 million Americans. Alzheimer\u27s has been characterized by the formation of beta-amyloid peptide plaques between nerve cells in the brain. Analysis of the three-dimensional tertiary protein structure is a challenge, but could result in better development of therapeutic and diagnostic tests. The knobsocket model simplifies the complexity of threedimensional packing of protein residues into an easily interpretable two-dimensional map. The resulting topology map of tertiary structure clearly indicates how the amino acid residues interact with each other as a group and individually. The local set of amino acid residues form a three member socket, while a non-local residue is defined as the knob that packs into the socket. The Alzheimer disease state has been shown to be caused by prion amyloids, and structural information about these amyloids have been solved for the protein crystals 2LMN and 2LMP. Using the knob-socket model, packing topology maps were constructed for these amyloid states. These topology maps identify potential areas on the exposed amyloid surface that could interaction with a diagnostic peptide to identify early stages of the disease. Also, the exposed edges offer areas of interaction to inhibit further extension of the prion state and therefore a potential therapeutic by preventing amyloid plaque growth. The next steps are to synthesize these peptides that target the amyloid structure and test their binding ability and inhibition of amyloid plaque accumulation text Similar works Full text Scholarly CommonsProvided a free PDF (195.62 KB) purcc-2875oai:scholarlycommons.pacific.edu:purcc-2875 Last time updated on July 17, 2020 This paper was published in Scholarly Commons. Having an issue? Is data on this page outdated, violates copyrights or anything else? Report the problem now and we will take corresponding actions after reviewing your request. Report Useful links Blog About CORE Contacts Cookies Privacy notice Accessibility Writing about CORE? Discover our research outputs and cite our work. CORE is a not-for-profit service delivered by The Open University and Jisc.
