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Adsorption of alpha amino acids at the water/goethite interface
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
2008 (English)In: Journal of Colloid Interface Science, ISSN 0021-9797, Vol. 319, no 2, 416-28 p.Article in journal (Refereed) Published
Abstract [en]

The adsorption of amino acids onto mineral surfaces plays an important role in a wide range of areas, e.g., low-temperature aqueous geochemistry, bone formation and protein-bone interactions. In this work, the adsorption of three alpha aminoacids (sarcosine, MIDA and EDDA) onto goethite (α-FeOOH) was studied as a function of pH and background electrolyte concentration at 25.0 °C, and the molecular structures of the surface complexes formed were analyzed by means of ATR-FTIR spectroscopy. The results showed that adsorption of alpha amino acids were strongly dependent on the functionality and structure of the ligands. No adsorption was detected for the zwitterionic sarcosine indicating that simple alpha amino acids without other ionizable and/or functional groups display insignificant affinity for mineral surfaces such as goethite. With respect to the more complex amino acids, which are surface reactive, the number and relative positions of carboxylate and amine groups determine the types of surface interactions. These interactions range from non-specific outer-sphere to specific inner-sphere interactions as shown by the MIDA and EDDA results, respectively. The results presented herein suggest that isomerically-selective adsorption might only occur for amino acids that are capable of specific surface interactions, either through site-specific hydrogen bonding or inner-sphere complexation.

Place, publisher, year, edition, pages
2008. Vol. 319, no 2, 416-28 p.
Keyword [en]
Adsorption, Amino acids, water/mineral interface, Goethite, ATR-FTIR spectroscopy
URN: urn:nbn:se:umu:diva-6920DOI: doi:10.1016/j.jcis.2007.11.046PubMedID: 18155715OAI: diva2:146590
Available from: 2008-01-31 Created: 2008-01-31 Last updated: 2011-01-10Bibliographically approved

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