Supramolecular surfaces for protein immobilisation.

Di Palma, Giuseppe ORCID: 0000-0002-5530-9107 (2020). Supramolecular surfaces for protein immobilisation. University of Birmingham. Ph.D.

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Abstract

Protein immobilisation represents nowadays one of the most challenging fields in science, and many technologies have been developed based on this idea. Biosensors, using the interaction of the protein with glucose, DNA, or antibody are only a few examples of the massive amount of applications related to the concept of protein immobilisation. Despite many signs of progress that have been made in this field, the best method to immobilise protein on the surface is still not well defined. The immobilisation of proteins on the surface is nowadays obtained mostly through chemical or physical adsorption. Both methods, even considering the considerable amount of applications that are possible to find nowadays, still present some disadvantages. The supramolecular chemistry has the potential to overcome all these problems in a very elegant, fast and straightforward way, implying the host-guest interaction between a scaffold molecule and a protein. According to this, the development of a protein immobilising technique on the surface represents one of the most challenging tasks nowadays. This work is focused on the study of supramolecular complex proteins-scaffold and on the conditions to reach a well-packed self-assembled monolayer of these scaffolds on a surface. This method, with better control of its physiological conditions, can be used for a deeper study on protein activity for the development of highly accurate biochips.

Type of Work: Thesis (Doctorates > Ph.D.)
Award Type: Doctorates > Ph.D.
Supervisor(s):
Supervisor(s)EmailORCID
Mendes, PaulaUNSPECIFIEDorcid.org/0000-0001-6937-7293
Tommasone, StefanoUNSPECIFIEDorcid.org/0000-0001-8577-2111
Licence: All rights reserved
College/Faculty: Colleges (2008 onwards) > College of Engineering & Physical Sciences
School or Department: School of Chemical Engineering
Funders: Engineering and Physical Sciences Research Council
Subjects: Q Science > QD Chemistry
T Technology > TP Chemical technology
URI: http://etheses.bham.ac.uk/id/eprint/10161

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