These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Probing the adjustments of macromolecules during their surface adsorption.
    Author: Jia P, He M, Gong Y, Chu X, Yang J, Zhao J.
    Journal: ACS Appl Mater Interfaces; 2015 Apr 01; 7(12):6422-9. PubMed ID: 25762185.
    Abstract:
    Thiol-terminated polymers poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC-SH), poly(N,N-isopropylacrylamide) (PNIPAM-SH), and poly(tert-butyl acrylate) (PtBA-SH) were synthesized, and the polymers were grafted on the gold surfaces of quartz crystal microbalance with dissipation (QCM-D) and surface plasmon resonance (SPR) sensor chips to form brushes. The grafting process of the polymer brushes as well as protein adsorption onto the brush layers was monitored by in situ QCM-D and SPR techniques. By examining the changes in frequency and dissipation factor as well as the value of ∂D/∂f from QCM-D measurements, different stages of the polymer grafting and protein adsorption are distinguished. The most interesting discovery is the conformation change of BSA protein adsorption from a weakly adsorbed native state to a strongly immobilized denatured state on the polymer brushes. The corresponding change in BSA adsorption from a reversible state to an irreversible state was confirmed by SPR measurements. The adsorption of protein on the polymer brushes' surface relies largely on interaction between the protein and the polymers, and the stronger hydrophilicity of the surfaces is proved to be more effective to suppress the protein adsorption. Analysis of the D-f plot of QCM-D measurements helps to characterize different binding strength of protein and the underlying polymer surface.
    [Abstract] [Full Text] [Related] [New Search]