Protein covalent immobilization via its scarce thiol versus abundant amine groups: Effect on orientation, cell binding domain exposure and conformational lability

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 134; pp. 73 - 80
• Main Authors: Ba, O.M., Hindie, M., Marmey, P., Gallet, O., Anselme, K., Ponche, A., Duncan, A.C.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2015
• Subjects: Adsorption; Amines - chemistry; Binding; Cell adhesive protein; Cold plasma treatment; Covalence; Exposure; Fibronectin; Fibronectins - chemistry; Grafting; Immobilization; Microscopy, Atomic Force; Polystyrene; Protein Conformation; Protein grafting; Protein immobilization; Proteins; Rinsing; Sulfhydryl Compounds - chemistry; Surface characterization; Surface chemistry; Surface Properties; Cold plasma treatment; Protein immobilization; Adsorption; Protein grafting; Cell adhesive protein; Polystyrene; Surface characterization; Fibronectin

•A polystyrene polymer surface was functionalized with reactive functional amine groups.•Two protein covalent linkage strategies were investigated via scarce protein thiol and abundant amine side groups.•Both covalent linkage strategies showed significantly increased retention strength of the immobi...