Self-Assembly of Multiply-Responsive Peptide Copolymers
Lead Research Organisation:
University of Reading
Department Name: Chemistry
Abstract
This project is focussed on the development of novel multiply-responsive peptide/polymer conjugates that can disrupt the formation of amyloid fibrils. Amyloidosis is responsible for many diseases such as type II diabetes, CJD and especially Alzheimers, of especial relevance to the aging population in the developed world. Amyloidosis is caused by the misfolding of proteins and peptides into fibrils. We will prepare novel materials based on fragments of the amyloid beta peptide (believed to be responsible for Alzheimer's). These will be coupled via recently-developed synthetic methods to responsive synthetic polymers and peptides. The aim is to prepare peptide copolymers that can bind to amyloid and disrupt fibrillisation. Conjugation of peptides with polymers enables materials to be prepared that have enhanced stability in vivo and the use of responsive polymers will enable targeted delivery in response to thermal or chemical stimuli. This is expected to lead to a range of novel materials with possible therapeutic applications.
Organisations
Publications
Amit M
(2012)
Conductance of amyloid ß based peptide filaments: structure-function relations
in Soft Matter
Castelletto V
(2010)
Self-assembly of an amyloid peptide fragment-PEG conjugate: lyotropic phase formation and influence of PEG crystallization
in Polymer Chemistry
Castelletto V
(2010)
PEGylated amyloid peptide nanocontainer delivery and release system.
in Langmuir : the ACS journal of surfaces and colloids
Castelletto V
(2011)
Tuning the self-assembly of the bioactive dipeptide L-carnosine by incorporation of a bulky aromatic substituent.
in Langmuir : the ACS journal of surfaces and colloids
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
(2011)
Self-assembly of Fmoc-tetrapeptides based on the RGDS cell adhesion motif
in Soft Matter
Castelletto V
(2011)
Influence of end-capping on the self-assembly of model amyloid peptide fragments.
in The journal of physical chemistry. B
Castelletto V
(2012)
Modulating self-assembly of a nanotape-forming peptideamphiphile with an oppositely charged surfactant
in Soft Matter
Castelletto V
(2013)
New RGD-peptide amphiphile mixtures containing a negatively charged diluent.
in Faraday discussions
Description | This highly successful grant led to the development of new hybrid materials containing polymers and peptides with potential applications in drug delivery and as supports for cell culture for regenerative medicine. |
Exploitation Route | By practitioners in the healthcare field, especially regenerative medicine and drug delivery |
Sectors | Healthcare,Pharmaceuticals and Medical Biotechnology |
Description | This project led to a large number of publications and extensive promotion at national and international conferences |
First Year Of Impact | 2008 |
Sector | Chemicals,Healthcare,Pharmaceuticals and Medical Biotechnology |
Impact Types | Societal |