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Int. J. Mol. Sci. 2018, 19(2), 365; https://doi.org/10.3390/ijms19020365

Size-Dependent Affinity of Glycine and Its Short Oligomers to Pyrite Surface: A Model for Prebiotic Accumulation of Amino Acid Oligomers on a Mineral Surface

1
Chemical Evolution Lab Unit, Earth-Life Science Institute (ELSI), Tokyo Institute of Technology, 2-12-1-IE-1 Ookayama, Meguro-ku, Tokyo 152-8550, Japan
2
School of Materials and Chemical Technology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 226-8502, Japan
3
Faculty of Environment and Information Studies, Keio University, 5322 Endo, Fujisawa-shi, Kanagawa 252-0882, Japan
*
Author to whom correspondence should be addressed.
Received: 30 November 2017 / Revised: 23 December 2017 / Accepted: 23 December 2017 / Published: 25 January 2018
(This article belongs to the Special Issue Atomic Force Microscopy for Biological Applications)
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Abstract

The interaction strength of progressively longer oligomers of glycine, (Gly), di-Gly, tri-Gly, and penta-Gly, with a natural pyrite surface was directly measured using the force mode of an atomic force microscope (AFM). In recent years, selective activation of abiotically formed amino acids on mineral surfaces, especially that of pyrite, has been proposed as an important step in many origins of life scenarios. To investigate such notions, we used AFM-based force measurements to probe possible non-covalent interactions between pyrite and amino acids, starting from the simplest amino acid, Gly. Although Gly itself interacted with the pyrite surface only weakly, progressively larger unbinding forces and binding frequencies were obtained using oligomers from di-Gly to penta-Gly. In addition to an expected increase of the configurational entropy and size-dependent van der Waals force, the increasing number of polar peptide bonds, among others, may be responsible for this observation. The effect of chain length was also investigated by performing similar experiments using l-lysine vs. poly-l-lysine (PLL), and l-glutamic acid vs. poly-l-glutamic acid. The results suggest that longer oligomers/polymers of amino acids can be preferentially adsorbed on pyrite surfaces. View Full-Text
Keywords: pyrite; mineral surface; atomic force microscopy; unbinding force measurements; glycine; oligo-glycines; peptides; single molecule interaction; origins of life pyrite; mineral surface; atomic force microscopy; unbinding force measurements; glycine; oligo-glycines; peptides; single molecule interaction; origins of life
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Afrin, R.; Ganbaatar, N.; Aono, M.; Cleaves II, H.J.; Yano, T.-A.; Hara, M. Size-Dependent Affinity of Glycine and Its Short Oligomers to Pyrite Surface: A Model for Prebiotic Accumulation of Amino Acid Oligomers on a Mineral Surface. Int. J. Mol. Sci. 2018, 19, 365.

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