engleski

Thermodynamics of anion binding by pentaphenylalanine in acetonitrile

Cyclic peptides represent a large and underexploited class of drug discovery candidates. Their improved metabolic stability and binding affinity, in comparison with linear analogues, result in greater resistance to enzymatic hydrolysis, increased bioavailability, and bioactivity. In the synthesis of cyclic peptides, the main factor that affects the yield of a ring- closure reaction is the conformational preorganization, i.e. the ability of a linear precursor to adopt quasi-cyclic conformation in which the N– and C– termini are in a close proximity. One approach to achieve that is to use templating agents, such as anions, that can bind to linear precursors as well as cyclic peptides. In the scope of this work, we studied the binding of inorganic anions to pentaphenylalanine methyl ester in acetonitrile by means of 1H NMR, fluorimetric, and CD titrations. In addition, we carried out the MD simulations to get insight into the structural changes which occur upon anion binding to pentapeptide.

anion binding ; circular dichroism ; MD simulation ; NMR ; thermodynamics

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