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The binding of anions on linear and cyclic homopeptides

In the recent past cyclic peptides have attracted an increasing interest due to their unique chemical and biological properties. Cyclic peptides exhibit improved metabolic stability and bioavailability as well as enhanced binding affinity and selectivity toward substrates compared to their more flexible linear analogs. These compounds can selectively bind anions and are capable of passing the hydrophobic lipid barriers which means they can be used as ion transporters. Furthermore, cyclic peptides can imitate biological systems and are excellent tools for understanding complex biological processes such as protein–protein and generally host–guest interactions. The main problem in the synthesis of this compounds is conformational preorganization which is needed to succesfully close the ring by reaction between N-terminus and C-terminus (head- to-tail cyclization). Previous research reports that anionic species play important role in this step by formation of complex with linear precursor. In our research among other methods we use classical MD simuations which can give us structural information about formed peptide-anion complexes to get insight into template effect of anion on head-to-tail macrocyclization.

homopeptides, MD simulations, anion binding

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