NDLI: Development of nonfouling polypeptides with uniform alternating charges by polycondensation of the covalently bonded dimer of glutamic acid and lysine

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Development of nonfouling polypeptides with uniform alternating charges by polycondensation of the covalently bonded dimer of glutamic acid and lysine

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Journal of Materials Chemistry B Vol -1

Development of nonfouling polypeptides with uniform alternating charges by polycondensation of the covalently bonded dimer of glutamic acid and lysine

Content Provider	Royal Society of Chemistry (RSC)
Author	Chen, Shengfu Yang, Qinghua Ma, Guanglong Yuan, Jiang Lin, Weifeng Wang, Longgang
Copyright Year	2014
Abstract	In this work, nonfouling polypeptides with homogenous alternating charges were synthesized by polycondensation of the covalently bonded dimer of glutamic acid (E) and lysine (K) (EK dimer) with benzyloxycarbonyl (Z)-protected side chains. This facile method successfully solved the uniformity problem of nonfouling peptides caused by the copolymerization of two different monomers and enabled the incorporation of various terminal functional groups for future applications. The molecular weights (MWs) of the nonfouling peptides can be easily controlled by the ratio of the terminal group, lipoic acid, to the EK dimer. The nonfouling peptides can form self-assembling monolayers (SAMs) on a gold surface through two terminal thiol groups, which were characterized by attenuated total reflection Fourier transform infrared (ATR-FTIR), X-ray photoelectron spectroscopy (XPS) and ellipsometry (ELL). The resistance to nonspecific protein adsorption, cell attachment and bacterial adhesion of these nonfouling peptide SAMs and the in vitro cytotoxicity and haemolytic activity of these peptides were also evaluated. The results show that the lowest relative protein adsorptions of antibody (anti-IgG) and fibrinogen (Fg) on the SAMs are 5.1 ± 1.6% and 7.3 ± 1.8%, respectively, determined by enzyme-linked immunosorbent assay (ELISA), where the protein adsorption on a tissue culture polystyrene (TCPS) surface was set to 100%. Almost no obvious cell attachment and bacterial adhesion were observed, and no cytotoxicity and no haemolytic activity in vitro were detected. With the advantages of biocompatibility, biodegradability and the abundance of moieties for ligand immobilization, these nonfouling peptides developed by the facile method can be used in a wide range of biomedical applications.
Starting Page	577
Ending Page	584
Page Count	8
File Format	HTM / HTML PDF
ISSN	2050750X
Volume Number	2
Issue Number	5
Journal	Journal of Materials Chemistry B
DOI	10.1039/c3tb21333a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Fourier Condensation reaction Protein dimer Carboxylic acid Lysine Thiol Fourier transform Infrared spectroscopy X-ray photoelectron spectroscopy Photoemission spectroscopy Ellipsometry Protein Adsorption Peptide Cytotoxicity Hemolysis Fibrinogen ELISA Tissue culture Polystyrene Biocompatibility Ligand
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Materials Science Biomedical Engineering

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