Cargando…

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

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 miner...

Descripción completa

Detalles Bibliográficos
Autores principales: Afrin, Rehana, Ganbaatar, Narangerel, Aono, Masashi, Cleaves, H. James, Yano, Taka-aki, Hara, Masahiko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5855587/
https://www.ncbi.nlm.nih.gov/pubmed/29370126
http://dx.doi.org/10.3390/ijms19020365
_version_ 1783307131695398912
author Afrin, Rehana
Ganbaatar, Narangerel
Aono, Masashi
Cleaves, H. James
Yano, Taka-aki
Hara, Masahiko
author_facet Afrin, Rehana
Ganbaatar, Narangerel
Aono, Masashi
Cleaves, H. James
Yano, Taka-aki
Hara, Masahiko
author_sort Afrin, Rehana
collection PubMed
description 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.
format Online
Article
Text
id pubmed-5855587
institution National Center for Biotechnology Information
language English
publishDate 2018
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-58555872018-03-20 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 Afrin, Rehana Ganbaatar, Narangerel Aono, Masashi Cleaves, H. James Yano, Taka-aki Hara, Masahiko Int J Mol Sci Article 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. MDPI 2018-01-25 /pmc/articles/PMC5855587/ /pubmed/29370126 http://dx.doi.org/10.3390/ijms19020365 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Afrin, Rehana
Ganbaatar, Narangerel
Aono, Masashi
Cleaves, H. James
Yano, Taka-aki
Hara, Masahiko
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
title 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_short 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
title_sort 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5855587/
https://www.ncbi.nlm.nih.gov/pubmed/29370126
http://dx.doi.org/10.3390/ijms19020365
work_keys_str_mv AT afrinrehana sizedependentaffinityofglycineanditsshortoligomerstopyritesurfaceamodelforprebioticaccumulationofaminoacidoligomersonamineralsurface
AT ganbaatarnarangerel sizedependentaffinityofglycineanditsshortoligomerstopyritesurfaceamodelforprebioticaccumulationofaminoacidoligomersonamineralsurface
AT aonomasashi sizedependentaffinityofglycineanditsshortoligomerstopyritesurfaceamodelforprebioticaccumulationofaminoacidoligomersonamineralsurface
AT cleaveshjames sizedependentaffinityofglycineanditsshortoligomerstopyritesurfaceamodelforprebioticaccumulationofaminoacidoligomersonamineralsurface
AT yanotakaaki sizedependentaffinityofglycineanditsshortoligomerstopyritesurfaceamodelforprebioticaccumulationofaminoacidoligomersonamineralsurface
AT haramasahiko sizedependentaffinityofglycineanditsshortoligomerstopyritesurfaceamodelforprebioticaccumulationofaminoacidoligomersonamineralsurface