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Surface functional group chemistry of intact Gram-positive and Gram-negative bacterial cells and their isolated cell walls was examined as a function of pH, growth phase, and growth media (for intact cells only) using attenuated total reflectance Fourier transform infrared (ATR-FTIR) spectroscopy. Infrared spectra of aqueous model organic molecules, representatives of the common functional groups found in bacterial cell walls (i.e., hydroxyl, carboxyl, phosphoryl, and amide groups), were also examined in order to assist the interpretation of the infrared spectra of bacterial samples. The surface sensitivity of the ATR-FTIR spectroscopic technique was evaluated using diatom cells, which possess a several-nanometers-thick layer of glycoprotein on their silica shells. The ATR-FTIR spectra of bacterial surfaces exhibit carboxyl, amide, phosphate, and carbohydrate related features, and these are identical for both Gram-positive and Gram-negative cells. These results provide direct evidence to the previously held conviction that the negative charge of bacterial surfaces is derived from the deprotonation of both carboxylates and phosphates. Variation in solution pH has only a minor effect on the secondary structure of the cell wall proteins. The cell surface functional group chemistry is altered neither by the growth phase nor by the growth medium of bacteria. This study reveals the universality of the functional group chemistry of bacterial cell surfaces.

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The effects of Al(2)O(3), TiO(2), and ZnO nanoparticles (NPs) on bacteria cells and bacterial surface biomolecules were studied by Fourier transform infrared (FTIR) spectroscopy. All the examined biomolecules showed IR spectral changes after NP exposure. Lipopolysaccharide and lipoteichoic acid could bind to oxide NPs through hydrogen bonding and ligand exchange, but the cytotoxicity of NPs seemed largely related to the function-involved or devastating changes to proteins and phospholipids of bacteria. The three NPs decreased the intensity ratio of β-sheets/α-helices, indicating protein structure change, which may affect cell physiological activities. The phosphodiester bond of L-α-phosphatidylethanolamine was broken by ZnO NPs, forming phosphate monoesters and resulting in the highly disordered alkyl chain. Such damage to phospholipid molecular structure may lead to membrane rupture and cell leaking, which is consistent with the fact that ZnO is the most toxic of the three NPs. The cell surface biomolecular changes revealed by FTIR spectra provide a better understanding of the cytotoxicity of oxide NPs.

Competitive adsorption between nonpolar organic compounds and polar ionic organic compounds (IOCs) on carbon nanotubes (CNTs) is essential for application of CNTs as superior sorbents and for environmental risk assessment of both CNTs and organic contaminants. It was observed in this study that adsorption of neutral and dissociated species of polar 2,4-dichlorophenol (DCP) and 4-chloroaniline (PCAN) on a multiwalled CNT sample (MWCNT15) can be suppressed by nonpolar naphthalene. Naphthalene adsorption can also be suppressed by neutral DCP/PCAN, but not dissociated DCP/PCAN. Moreover, competition of naphthalene decreased the adsorption affinity of neutral DCP/PCAN, but not their adsorption capacity because of the formation of solute bilayer on MWCNT15. For dissociated DCP/PCAN, naphthalene not only decreased their adsorption affinity but also their adsorption capacity because no solute bilayer was formed. Neutral DCP/PCAN also decreased the adsorption affinity and adsorption capacity of naphthalene. These observations indicate that competitive adsorption of naphthalene with DCP/PCAN depends on the dissociation of DCP/PCAN, as interpreted by (i) the different sites on CNTs for adsorption of organic chemicals (i.e., naphthalene, and the neutral and dissociated species of DCP/PCAN), (ii) the interactions between organic chemicals, and (iii) the interactions of organic chemicals with CNT surface.

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Although nanoparticle/protein binding and the cytotoxicity of nanoparticles have been separately reported, there has been no study linking the nature of nanoparticle/protein clusters to cell uptake and the dynamic cellular responses. We report here that water-soluble iron oxide-based magnetic nanoparticles (MNPs) with different sizes and surface chemistry bind different serum proteins in terms of protein identity and quantity without changing the protein secondary structures. Carboxylated MNPs (and aminated one in smaller MNPs) resulted in higher cytotoxicity, and PEG coating reduced both cell uptake and the cytotoxicity. Smaller MNPs (especially the carboxylated one) bind more serum proteins, are much less taken up by cells as compared to larger particles, and yet elicit more dynamic cytotoxic responses. Besides the intrinsic effects of size and surface charge of the water-soluble MNPs, the cellular effects of MNPs/protein clusters were also attributed to the identity and quantity of the adsorbed proteins rather than the binding-induced new epitopes on the proteins.