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An Intrinsic Hydrophobicity Scale for Amino Acids and Its Application to Fluorinated Compounds

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Hoffmann,  Waldemar
Freie Universität Berlin, Department of Biology, Chemistry and Pharmacy;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Langenhan,  Jennifer
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Chang,  Rayoon
Freie Universität Berlin, Department of Biology, Chemistry and Pharmacy;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Seo,  Jongcheol
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Meijer,  Gerard
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Pagel,  Kevin
Freie Universität Berlin, Department of Biology, Chemistry and Pharmacy;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Citation

Hoffmann, W., Langenhan, J., Huhmann, S., Moschner, J., Chang, R., Accorsi, M., et al. (2019). An Intrinsic Hydrophobicity Scale for Amino Acids and Its Application to Fluorinated Compounds. Angewandte Chemie International Edition, 58(24), 8216-8220. doi:10.1002/anie.201813954.


Cite as: http://hdl.handle.net/21.11116/0000-0003-58AB-A
Abstract
The classification of amino acids according to their intrinsic properties, such as the physico‐chemical properties and structure, yields fundamental insights into their role in interactions in biological processes. More than 100 hydrophobicity scales have been introduced, with each being based on a distinct condensed‐phase approach. However, a comparison of the hydrophobicity values gained from different techniques, and their relative ranking is not straightforward, as the interactions between the environment and amino acid are unique to each method. Here, we overcome this limitation by studying the properties of amino acids in the clean‐room environment of the gas phase. In the gas phase, entropic contributions from the hydrophobic effect are by default absent and only the side‐chain´s polarity dictates self‐assembly. This allows for the derivation of a novel hydrophobicity scale, which is solely based on the interaction between individual amino acid units within the cluster and thus more accurately reflects the intrinsic nature of a side‐chain. This principle can be further applied to classify non‐natural derivatives, as shown here for fluorinated amino acid variants.