Specific binding of immunoglobulin G with bioactive short peptides supported on antifouling copolymer layers for detection in quartz crystal microgravimetry and surface plasmon resonance.

A new peptide-based system supported on copolymer brushes grafted from gold sensors and with resistance to nonspecific adsorption is reported for selective binding of human immunoglobulin G (IgG). A random copolymer rich in primary amines, poly(2-aminoethyl methacrylate hydrochloride-co-2-hydroxyethyl methacrylate) (poly(AMA-co-HEMA)) was first grafted from initiator-coated gold substrates via activators regenerated by electron transfer-atom transfer radical polymerization (ARGET-ATRP), followed by immobilization of acetylated-HWRGWVA peptide, which has specific binding affinity with IgG. The peptide ligands covalently linked to the soft copolymer layer were characterized by X-ray photoelectron spectroscopy (XPS), water contact angle, ellipsometry, and atomic force microscopy (AFM). The extent of binding, binding affinity, and selectivity for target IgG molecules as well as the capability to minimize nonspecific interactions with other proteins were examined by fluorescence imaging, surface plasmon resonance (SPR), and quartz crystal microgravimetry (QCM). The effect of copolymer molecular composition and analyte concentration was elucidated in order to design systems based on immobilized peptides for high signal-to-noise response and detection limits that meet the requirements for IgG biosensing in fluid matrixes.