Self-assembly of GFP-HMPA protein polymer conjugates: Effect of polymer hydrophobicity


Conjugation of therapeutic proteins to polymers is well established but most methods result in multi-site and multiple conjugation, crosslinking resulting in lack of orientation and loss of activity. Using an enzyme mediated conjugation methodology we have prepared well-defined protein-polymer conjugates using a model protein, green fluorescent protein with an amphiphilic, temperature responsive diblock copolymer based on N-2-hydroxypropyl methacrylamide, a polymer commonly used for delivery of therapeutics. In this proposal we wish to determine the effects of polymer hydrophobicity on the properties of aggregates formed by these polymers & conjugates in solution, to develop an understanding of the phase behaviour of these species. Since one of the polymer blocks becomes less soluble as the temperature increases we will also study the effect of temperature on these self-assembled species

Metadata Access
Creator Ms Duygu Celebi; Dr Gavin Hazell; Dr Ilaria Idini; Dr Gabriel Cavalli; Dr Susanna Piluso; Professor Karen Edler; Dr Amani El Fagui; Dr Heather Cassell
Publisher ISIS Neutron and Muon Source
Publication Year 2016
Rights CC-BY Attribution 4.0 International;
OpenAccess true
Contact isisdata(at)
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2013-03-26T00:00:00Z
Temporal Coverage End 2013-08-01T08:02:49Z