Amyloid Peptide Conjugates: Visit to Argentina to Develop Collaboration
Lead Research Organisation:
University of Reading
Department Name: Chemistry
Abstract
We propose to initiate a collaborative programme to examine the effect of peptide/polymer conjugates on amyloid fibrillisation in vitro and in vivo. The conjugates are expected to bind to amyloid and to disrupt fibrillisation. Members of the Reading team will visit Instituto Leloir (Buenos Aires, Argentina) to perform cell viability/cytotoxicity experiments. The Instituto Leloir was founded by the Nobel laureate Luis Federico Leloir and is one of the premier institutions devoted to biochemistry in South America, indeed it has a leading international profile. Members of the Leloir team will visit Reading for x-ray, neutron and electron microscopy experiments. Diseases such as Alzheimer's and type II diabetes are of increasing importance to the aging population in the developed world. They result result from the formation of amyloid in which proteins and peptides form fibrils based on a beta-sheet structure in which the peptide backbone is orthogonal to the fibril axis (cross beta structure). We propose to initiate a collaborative programme to examine the effect of peptide/polymer conjugates on amyloid fibrillisation in vitro and in vivo. The conjugates are expected to bind to amyloid and to disrupt fibrillisation in a stimuli-responsive fashion. The human amyloid peptide, Abeta is implicated in Alzheimers.
Publications
Amit M
(2012)
Conductance of amyloid ß based peptide filaments: structure-function relations
in Soft Matter
Castelletto V
(2012)
Control of strand registry by attachment of PEG chains to amyloid peptides influences nanostructure
in Soft Matter
Castelletto V
(2010)
A beta-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid beta-peptide.
in Journal of peptide science : an official publication of the European Peptide Society
Castelletto V
(2010)
A beta-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid beta-peptide.
in Journal of peptide science : an official publication of the European Peptide Society
De Tullio MB
(2013)
Proteolytically inactive insulin-degrading enzyme inhibits amyloid formation yielding non-neurotoxic aß peptide aggregates.
in PloS one
Description | This grant funded travel to Argentina as part of a collaboration which led to publications concerning amyloid, relevant to insulin activity and diabetes |
Exploitation Route | May be relevant to medicial practitioners |
Sectors | Healthcare Pharmaceuticals and Medical Biotechnology |
Description | Two publications resulting from this collaborative travel grant |
First Year Of Impact | 2009 |
Sector | Healthcare,Pharmaceuticals and Medical Biotechnology |
Impact Types | Societal |
Description | Senexis Ltd Cambridge |
Organisation | Senexis Ltd Cambridge |
Country | United Kingdom |
Sector | Private |
Start Year | 2009 |