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Affinity and Selectivity of Peptides for Inorganic Materials: A Thermodynamic Discussion of the Role of Conformational Flexibility

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Abstract

The recognition of inorganic materials by polypeptides is a technologically relevant and scientifically intriguing phenomenon. Several features of the polypeptide determine the affinity for a given surface and, possibly, its selectivity among a set of materials or among various crystal planes of the same material. Different amino acids have different intrinsic affinities for a given surface; the geometrical features of the surface are also relevant in the recognition process. By means of a minimal, analytically solvable thermodynamic model for the polypeptide-surface interaction, we discuss the role of the conformational flexibility in determining affinity and selectivity of polypeptides for surfaces. In particular, the interplay between geometrical matching of polypeptide-surface features and the presence in the polypeptide of amino acids able to bind the target surface is analyzed as a function of the flexibility. A discussion of literature data in the light of this minimal model is also given.

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Notes

  1. One letter codes for amino acids mentioned in the text: W: tryptophan; A: alanine; R: arginine; L: leucine; S: serine; I: isoleucine; Q: glutamine; P: proline; Y: tyrosine; M: methionine.

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Acknowledgements

The author would like to thank MIUR under PRIN project 2012A7LMS3_003 and CNR under the flagship project NanoBrain.

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  1. Center S3, CNR Institute of Nanoscience, Modena, Italy

    Stefano Corni

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  1. Stefano Corni
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Correspondence to Stefano Corni.

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Corni, S. Affinity and Selectivity of Peptides for Inorganic Materials: A Thermodynamic Discussion of the Role of Conformational Flexibility. JOM 67, 781–787 (2015). https://doi.org/10.1007/s11837-015-1334-7

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  • DOI: https://doi.org/10.1007/s11837-015-1334-7

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