Abstract
A combination of in situ and ex situ surface plasmon resonance (SPR) imaging experiments is used to characterize the differential electrostatic adsorption of proteins and synthetic polypeptides onto photopatterned monolayers at gold surfaces. The nonspecific electrostatic adsorption of proteins onto negatively charged self-assembled monolayers (SAMs) of 11-mercaptoundecanoic acid (MUA) is found to depend on the protein pI, solution ionic strength, and solution pH. The pH dependence of the electrostatic adsorption of the protein avidin onto a MUA SAM indicates that a full monolayer adsorbs at a solution pH greater than 5.0, and an "effective pK(a)" of 3.6 is determined for the avidin adsorption. This effective pK(a) is a combination of the pK(a) of the MUA monolayer and the ion pairing adsorption coefficient for the avidin. Additional SPR imaging experiments show that the electrostatic adsorption of the synthetic polypeptide poly-l-lysine (PL) onto a MUA SAM varies with molecular weight, forming a full PL monolayer for polypeptides with more than 67 lysine residues.
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