engleski

Thermodynamic and structural studies on the complexation of methyl ester of pentaisoleucine with anions in acetonitrile

Over the past few decades anion receptors have attracted increasingly more interest in the field of supramolecular chemistry. Particularly interesting receptors are cyclic peptides. They have good complexation properties due to the extraordinary donor properties of the amide groups 1 , the flexibility of the macrocyclic ring and the variability of the subunits.[2] Cyclic peptides are formed by cyclization from linear analogs in which a conformationally more rigid macrocyclic ligand is formed from a flexible chain. The main factor that affects successful ring closure is the conformational preorganization, which is the ability of a linear precursor to bring its reactive termini in close spatial proximity. This can be achieved by using favorable template ions. Determination of the stability constants for the anion-receptor complexes of linear peptides can be useful for the determination of the best template agent in macrocyclization reaction. 3 In this work, binding affinities of pentaisoleucine methyl ester with several anions in acetonitrile were studied using 1 H NMR and ITC titrations as well as classical molecular dynamics simulations. 1 S. Kubik, Acc. Chem. Res. 2017, 50, 2870. 2 R. B. P. Elmes, K. A. Jolliffe, Chem. Commun. 2015, 51, 4951. 3 N. Vidović, G. Horvat, D. Riva, T. Rinkovec, N. Cindro, V. Tomišić, G. Speranza, Org. Lett. 2020, 22, 2129.

linear peptide ; anion binding ; acetonitrile

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