title: Structural influence of graft and block polycations on the adsorption of BSA.
abstract: Protein adsorption is considered as an important factor for the low transfection efficiency of polycations in vivo. In this study, two typical polycations of equal molecular weight with different structures were chosen to investigate their adsorption on bovine serum albumin (BSA), including the block copolymer named poly (N-vinylpyrrolidone)-b-poly (2-dimethylaminoethyl methacrylate) (PVP-b-PDMAEMA, i.e. PbP) and graft copolymer named PVP-g-PDMAEMA (PgP), respectively. Fluorescence spectroscopy was used to confirm the binding constants and binding sites between polycations and BSA in static state. The binding constants were 4.1×10(4)M(-1) vs 8.3×10(4)M(-1) and binding sites were 0.3 vs 1.1 for PbP and PgP, respectively, indicating PgP had stronger binding affinity with BSA. Surface plasmon resonance (SPR) was used to study the dynamical non-specific interaction between BSA and polycations as well as the polyplexes. The numbers of both PbP and PgP adsorbed on BSA increased with concentration of polycations increasing, and the number of PgP adsorbed on BSA is higher compared with PbP when their concentration is low. When their concentration is high, the number of PbP adsorbed on BSA is more than that of PgP. However, PgP/DNA polyplexes showed higher adsorption amount compared with PbP/DNA polyplexes at different N/P ratios.
authors.affiliation: School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
authors.forename: Li
authors.initials: L
authors.lastname: Zhang
authors.affiliation: School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
authors.forename: Fengmin
authors.initials: F
authors.lastname: Jin
authors.affiliation: School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
authors.forename: Tingbin
authors.initials: T
authors.lastname: Zhang
authors.affiliation: School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China. Electronic address: lingzhang@tju.edu.cn.
authors.forename: Ling
authors.initials: L
authors.lastname: Zhang
authors.affiliation: School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China; Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, China. Electronic address: jinfengxing@tju.edu.cn.
authors.forename: Jinfeng
authors.initials: J
authors.lastname: Xing
mesh_terms: D000327:Adsorption; D004247:DNA / Q000737:chemistry; D007700:Kinetics; D008958:Models, Molecular; D015394:Molecular Structure; D011073:Polyamines / Q000737:chemistry*; D000071228:Polyelectrolytes; D011108:Polymers / Q000737:chemistry; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D020349:Surface Plasmon Resonance
chemical_list: D004247:DNA; D011073:Polyamines; D000071228:Polyelectrolytes; D011108:Polymers; D012710:Serum Albumin, Bovine
keywords: Bovine serum albumin; Fluorescence spectrum; Gene delivery; Polycations; Surface plasmon resonance