Immobilisation of bovine serum albumin on graphene oxide through covalent and noncovalent interactions
Year: 2025
Type: article
Abstract: Developing robust, user-friendly platforms for protein and enzyme immobilisation is a key challenge in biomedical and industrial fields. Graphene oxide (GO) has emerged as a promising support for immobilising various biomolecules. This study explores both covalent and noncovalent immobilisation of bovine serum albumin (BSA) onto GO under varying conditions. Noncovalent immobilisation at different pH levels relies on electrostatic and hydrophobic interactions, hydrogen bonding, and van der Waals forces to form the GO-BSA complex. Covalent immobilisation involves activating GO’s carboxyl groups with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. hydrochloride (EDC) and stabilising with N-hydroxysuccinimide (NHS) to produce functionalised GO (FGO), which reacts with BSA’s amine groups to form FGO-BSA conjugates. X-ray photoelectron spectroscopy (XPS) confirmed covalent binding through the detection of amide bonds and aromatic nitrogen. Interestingly, XPS also revealed higher BSA loading in GO-BSA (noncovalent) compared to FGO-BSA (covalent) under acidic conditions. Bradford assays further showed that GO can adsorb up to 80% of introduced BSA via both immobilisation methods. • Graphene oxide adsorbs more than 70% of introduced BSA to the dispersion via covalent and noncovalent interactions. • Adsorption of bovine serum albumin onto graphene oxide and functionalised graphene oxide was higher in acidic environment than that in neutral one. • Loading of bovine serum albumin on graphene oxide was higher in the case of noncovalent immobilisation relative to covalent one under acidic conditions, however; the interactions were weaker.
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,790
OpenAlex ID: W4415225085