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Issue 3, 2015
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A thermodynamic insight into the recognition of hydrophilic and hydrophobic amino acids in pure water by aza-scorpiand type receptors

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Abstract

Interactions of different hydrophilic (His, Asp, Glu,) and hydrophobic (Ala, Phe, Tyr, Trp) amino acids in water with a scorpiand aza-macrocycle (L1) containing a pyridine group in the ring and its derivative (L2) bearing a naphthalene group in the tail have been analysed by potentiometric and calorimetric measurements. Theoretical calculations corroborate that major attractive forces that hold the adduct together are hydrogen bonds and salt-bridges, even though other interactions such as π-stacking or NH+⋯π may contribute in the case of hydrophobic amino acids and L2. Calorimetric measurements indicate that the interactions between L1 and the different amino acids are principally driven by entropy, often associated with solvation/desolvation processes.

Graphical abstract: A thermodynamic insight into the recognition of hydrophilic and hydrophobic amino acids in pure water by aza-scorpiand type receptors

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Publication details

The article was received on 30 Sep 2014, accepted on 30 Oct 2014 and first published on 30 Oct 2014


Article type: Paper
DOI: 10.1039/C4OB02092H
Citation: Org. Biomol. Chem., 2015,13, 843-850
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    A thermodynamic insight into the recognition of hydrophilic and hydrophobic amino acids in pure water by aza-scorpiand type receptors

    S. Blasco, B. Verdejo, C. Bazzicalupi, A. Bianchi, C. Giorgi, C. Soriano and E. García-España, Org. Biomol. Chem., 2015, 13, 843
    DOI: 10.1039/C4OB02092H

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