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Τύπος: Αναρτημένη ανακοίνωση (poster)
Τίτλος: A novel approach to design and dynamically measure in vitro the biological activity of IAPP analogues designed by ancestral gene reconstruction for more efficient treatment of diabetes type-2
Εναλλακτικός τίτλος: Μια καινοτόμος προσέγγιση σχεδίασης και δυναμικής μέτρησης, σε in vitro συστήματα και σε 3D καλλιέργειες β-κυττάρων του παγκρέατος, της βιολογικής ενεργότητας IAPP αναλόγων που σχεδιάστηκαν μέσω της ανασυγκρότησης αρχέγονων αλληλουχιών για την πιο αποτελεσματική θεραπεία του διαβήτη τύπου-2
Συγγραφέας: [EL] Γεωργούλης, Αναστάσιος[EN] Georgoulis, Anastasios
[EL] Παπαγεωργίου, Άννα[EN] Papageorgiou, Anna
[EL] Αδάμ, Παναγιώτης[EN] Adam, Panagiotis
[EL] Βοργιάς, Κωνσταντίνος[EN] Vorgias, Constantinos
Ημερομηνία: Νοε-2018
Περίληψη: Under abnormal conditions, many proteins are unable to obtain or maintain their native fold and are driven to a misfolded state. Misfolded proteins self-assemble either to amorphous or to organized aggregates known as amyloid fibrils. In humans, amyloid fibrils can be accumulated on the surface of any organ or tissue and lead to conformational diseases known as amyloidoses. Type-2 diabetes (T2D), recorded in 350 million people, is caused by the deposition of the amylin peptide (IAPP) in pancreatic islets. This deposition reduce and complete eliminate the mass of β-pancreatic cells leading to disturbances in insulin secretion. The aim of this project is to design novel non-amyloidogenic IAPP analogs using the promising phylogenetic approach of ancestral gene reconstruction. A novel in vitro transcription-translation system has been developed in our group to monitor the kinetics at the early stages of aggregation of IAPP, since as oligomers are very toxic. Eucaryotic expression vector has been engineered to produce, in a cell free system of HeLa extracts, various IAPP peptide analogs linked to the fluorescent protein eGFP. With this experimental approach, if amyloidogenic IAPP will form fibrils much faster than the folding of eGFP will not allow the correct folding of eGFP and no fluorescence can be measured. If IAPP analogs that either do not form fibrils or form fibrils at rates much lower than the rate of folding of eGFP will allow eGFP to fold correctly and emit fluorescence. The results showed differences in the oligomers formation of IAPP analogs through the fluorescence by the eGFP. We also confirmed the oligomers formation using size-exclusion chromatography coupled to a fluorescence detector. Therefore, novel IAPP analogs that may stop the whole cascade at the nucleation phase, will shed light to the mechanism of amyloid formation and provide a basis for more efficient treatment of T2D.
Γλώσσα: Αγγλικά
Τόπος δημοσίευσης: Λάρισα, Ελλάδα
Σελίδες: 1
Θεματική κατηγορία: [EL] Βιοχημεία και Μοριακή βιολογία[EN] Biochemistry and Molecular Biology
Λέξεις-κλειδιά: diabetesamyloidosisamylin
Κάτοχος πνευματικών δικαιωμάτων: © by the author(s)
Όνομα εκδήλωσης: 69o Πανελλήνιο Συνέδριο Ελληνικής Εταιρείας Βιοχημείας & Μοριακής Βιολογίας
Τοποθεσία εκδήλωσης: Λάρισα, Ελλάδα
Ημ/νία έναρξης εκδήλωσης: 23-Νοε-2018
Ημ/νία λήξης εκδήλωσης: 25-Νοε-2018
Σημειώσεις: Poster P121 - 69thPanhellenic Conference of the Hellenic Society for Biochemistry and Molecular Biology (HSBMB)
Conference Programme : https://eebmb2018.gr/wp-content/uploads/2018/11/EEBMB2018-Programme-Preview-3.pdf
This work was carried out within the framework of "Support of postdoctoral researchers" of "Development of Human Resources, Education and Lifelong Learning" 2014-2020 which is being implemented from State Scholarships Foundation (IKY) and was co-funded by the European Social Fund and Greek public.
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