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  • Title: An investigation of the influence of chain length on the interfacial ordering of L-lysine and L-proline and their homopeptides at hydrophobic and hydrophilic interfaces studied by sum frequency generation and quartz crystal microbalance.
    Author: York RL, Holinga GJ, Somorjai GA.
    Journal: Langmuir; 2009 Aug 18; 25(16):9369-74. PubMed ID: 19719227.
    Abstract:
    Sum frequency generation vibrational spectroscopy (SFG) and quartz crystal microbalance with dissipation monitoring (QCM-D) are employed to study the interfacial structure and adsorbed amount of the amino acids L-lysine and L-proline and their corresponding homopeptides, poly-L-lysine and poly-L-proline, at two liquid-solid interfaces. SFG and QCM-D experiments of these molecules are carried out at the interface between phosphate buffered saline at pH 7.4 (PBS) and the hydrophobic deuterated polystyrene (d8-PS) surface as well as the interface between PBS and hydrophilic fused silica (SiO2). The SFG spectra of the amino acids studied here are qualitatively similar to their corresponding homopeptides; however, the SFG signal from amino acids at the solid/PBS interface is smaller in magnitude relative to their more massive homopeptides at the concentrations studied here. Substantial differences are observed in SFG spectra for each species between the hydrophobic d8-PS and the hydrophilic SiO2 liquid-solid interfaces, suggesting surface-dependent interfacial ordering of the biomolecules. Over the range of concentrations used in this study, QCM-D measurements also indicate that on both surfaces poly-L-lysine adsorbs to a greater extent than its constituent amino acid L-lysine. The opposite trend is demonstrated by poly-L-proline which sticks to both surfaces less extensively than its corresponding amino acid, L-proline. Lastly, we find that the adsorption of the molecules studied here can have a strong influence on interfacial water structure as detected in the SFG spectra.
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