Biotechnological applications of a surfactant protein, ranaspumin-2

Desai, Vibhuti H. (2017) Biotechnological applications of a surfactant protein, ranaspumin-2. PhD thesis, University of Glasgow.

Full text available as:
[thumbnail of 2017DesaiPhD.pdf] PDF
Download (5MB)
Printed Thesis Information: https://eleanor.lib.gla.ac.uk/record=b3290635

Abstract

Surfactant activity is generally associated with small molecules rather than biological macromolecules like proteins. Only a few proteins have good intrinsic surfactant activity, an example being the natural surfactant ranaspumin 2 (Rsn2) from the foam nests of the tĂșngara frog. In solution, Rsn2 has a hydrophobic core and hydrophilic exterior, but when Rsn2 comes in contact with an air-water interface, it changes conformation to expose its hydrophobic core to interact with the air and present a hydrophilic face to the water. The unique combination of biocompatibility along with surface activity offers the possibility of developing biomedical applications based on Rsn2. Some of the possible applications, including cell patterning, functionalising scaffolds and stabilising droplets, have been explored in the work described in this thesis.

The ability of Rsn2 to coat hydrophobic surfaces persistently, rendering them wettable and the nature of coating and interaction with the surfaces were investigated. This formed the basis for the development of a method to coat a range of hydrophobic polymers, which are commonly used for biomedical applications. These Rsn2 coated surfaces were tested for their capability to control cell adhesion on surfaces which usually do not support cell adhesion. Rsn2 coating was demonstrated to promote, and thus allowed the spatial control over, cell adhesion on otherwise non-cell compatible surfaces.

The potential of Rsn2 to be used as a protein fusion partner for the production of further functionalised cell engineering substrates was explored by constructing five different integrin binding sequence (IBS)-Rsn2 conjugates. Specific IBS-Rsn2 proteins proved successful in increasing the adhesion and biomineralising potential of osteoblasts isolated from neonatal rats.

In addition, Rsn2's ability to stabilise microscopic oil droplets were investigated. Rsn2 stabilised oil droplets were stable for more than six months.

Thus, the surfactant properties of Rsn2 can be used for many potential biomedical applications.

Item Type: Thesis (PhD)
Qualification Level: Doctoral
Keywords: Ranaspumin 2 (Rsn2), cell patterning, functionalising scaffolds using integrin binding sequences, stabilising oil droplets emulsions, the major extrapallial fluid protein.
Subjects: Q Science > QH Natural history > QH345 Biochemistry
Colleges/Schools: College of Medical Veterinary and Life Sciences > School of Molecular Biosciences > Molecular Biosciences
Supervisor's Name: Smith, Dr. Brian
Date of Award: 2017
Depositing User: Dr. Vibhuti Desai
Unique ID: glathesis:2017-8609
Copyright: Copyright of this thesis is held by the author.
Date Deposited: 05 Dec 2017 11:42
Last Modified: 02 Apr 2019 13:19
URI: https://theses.gla.ac.uk/id/eprint/8609

Actions (login required)

View Item View Item

Downloads

Downloads per month over past year