A thermodynamic insight into the recognition of hydrophilic and hydrophobic amino acids in pure water by aza-scorpiand type receptors. Issue 3 (14th November 2014)

• Record Type: Journal Article
• Authors: Blasco, Salvador; Verdejo, Begoña; Bazzicalupi, Carla; Bianchi, Antonio; Giorgi, Claudia; Soriano, Concepción; García-España, Enrique
• Is Part Of: Organic & biomolecular chemistry. Volume 13:Issue 3(2015)
• Page Start: 843
• Page End: 850
• Publication Date: 2014-11-14
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c4ob02092h
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : Thermodynamic studies about the interaction of scorpiand aza-macrocycles with amino acids in water show entropy driven stabilisations often associated with solvation/desolvation processes. 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 andL2 . Calorimetric measurements indicate that the interactions betweenL1 and the different amino acids are principally driven by entropy, often associated with solvation/desolvation processes.