Cation-based approach to morphological diversity of diphenylalanine dipeptide structures

Abstract

Different approaches are taken in order to examine the spontaneous arrangement processes of dipeptide structures. One of these approaches is to examine the effects of common cations on dipeptide structures’ self-assembly processes. In this study, the effects of Al³⁺, Cu²⁺, Pb²⁺, Hg²⁺, Mg²⁺, Zn²⁺, Cd²⁺, Fe²⁺ and Ni²⁺ cations on the self-assembly processes of diphenylalanine (FF) dipeptide molecules were investigated. A detailed examination was made of the self-assembly of FF dipeptides in the presence of Hg²⁺, and a spherical architecture structure was shown. The morphological diversity resulting from the effects of Hg²⁺ cations at different concentrations on FF dipeptides was explained using Scanning Electron Microscopy (SEM), X-ray Diffraction, (XRD), and Fourier Transform Infrared Spectroscopy (FTIR) techniques. It is thought that this work will contribute to the indexing of the effects of toxic species such as Hg²⁺ on dipeptides, which are the smallest peptide units obtained. We think that the examination of FF dipeptides in the structures of amyloid plaques, which are thought to affect neurological disorders such as Alzheimer's and Parkinson's, will prompt further studies.