University of Health Sciences Turkey, Gülhane Faculty of Pharmacy, Department of Pharmaceutical Chemistry, 06018 Ankara, Turkey.
Soft Matter. 2021 May 26;17(20):5221-5230. doi: 10.1039/d1sm00083g.
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.
为了研究二肽结构的自发排列过程，人们采用了不同的方法。其中一种方法是研究常见阳离子对二肽结构自组装过程的影响。在本研究中，研究了 Al3+、Cu2+、Pb2+、Hg2+、Mg2+、Zn2+、Cd2+、Fe2+和 Ni2+等阳离子对二苯丙氨酸（FF）二肽分子自组装过程的影响。详细研究了 Hg2+存在下 FF 二肽的自组装，显示出球形结构。使用扫描电子显微镜 (SEM)、X 射线衍射 (XRD) 和傅里叶变换红外光谱 (FTIR) 技术解释了 Hg2+阳离子在不同浓度下对 FF 二肽的影响所导致的形态多样性。我们认为这项工作将有助于了解 Hg2+等有毒物质对最小肽单元二肽的影响。我们认为，对淀粉样斑块结构中的 FF 二肽进行研究，将促使对阿尔茨海默病和帕金森病等神经紊乱产生进一步的研究。
