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Lookup NU author(s): Dr Djurdja Vukajlovic, John Sanderson, Professor David XieORCiD, Dr Tarek Abdelghany, Emma Smith, Dr Wing Man LauORCiD, Dr Keng Wooi NgORCiD, Professor Katarina NovakovicORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
The interaction between genipin and a model protein bovine serum albumin (BSA), with and without the addition of acetic acid, has been studied experimentally and by modelling. The number of amino groups available to react was determined to be 5.6 % of the total number of amino acid building blocks on BSA. Fluorescence intensity was used to record the progress of the reaction over the 24 h, while the modelling study focused on capturing the kinetic profiles of the reaction. The experiments revealed a slow start to the BSA and genipin interaction, that subsequently accelerated in an S-shaped curve which the modelling study linked with the existence of the feedback cycle for both reactive amino groups and genipin. At BSA concentrations ≥30 mg/mL the reaction was accelerated in the presence of acid, while below 30 mg/mL the acidified conditions delayed the onset of the reaction. Contrary to the reaction mechanisms previously proposed, a degree of breakdown of the fluorescent links in the products formed was denoted both experimentally and in a modelling study. This indicated the reversibility of the processes forming fluorescent product/s and suggested feasibility of the successful release of the protein following prospective encapsulation within the genipin-crosslinked hydrogel structure.
Author(s): Vukajlovic D, Timmons R, Macesic S, Sanderson J, Xie F, Abdelghany TM, Smith E, Lau WM, Ng KW, Novakovic K
Publication type: Article
Publication status: Published
Journal: International Journal of Biological Macromolecules
Year: 2024
Volume: 276
Issue: Part 1
Print publication date: 01/09/2024
Online publication date: 14/07/2024
Acceptance date: 11/07/2024
Date deposited: 02/08/2024
ISSN (print): 0141-8130
ISSN (electronic): 1879-0003
Publisher: Elsevier BV
URL: https://doi.org/10.1016/j.ijbiomac.2024.133850
DOI: 10.1016/j.ijbiomac.2024.133850
Data Access Statement: Data will be made available on request.
PubMed id: 39004259
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