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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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Supplementary files

Article information


Submitted
30 Sep 2014
Accepted
30 Oct 2014
First published
30 Oct 2014

This article is Open Access

Org. Biomol. Chem., 2015,13, 843-850
Article type
Paper

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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