About cookies on this site Our websites require some cookies to function properly (required). In addition, other cookies may be used with your consent to analyze site usage, improve the user experience and for advertising. For more information, please review your options. By visiting our website, you agree to our processing of information as described in IBM’sprivacy statement. To provide a smooth navigation, your cookie preferences will be shared across the IBM web domains listed here.
Publication
Journal of Chemical Physics
Paper
Exploring biological effects of MoS2 nanosheets on native structures of α-helical peptides
Abstract
Recent reports of mono- and few-layer molybdenum disulfide (MoS2), a representative transition metal dichacogenide (TMD), as antibacterial and anticancer agents have shed light on their potential in biomedical applications. To better facilitate these promising applications, one needs to understand the biological effects of these TMDs as well, such as their potential adverse effects on protein structure and function. Here, we sought to understand the interaction of MoS2 nanosheets with peptides using molecular dynamics simulations and a simple model polyalanine with various lengths (PAn, n = 10, 20, 30, and 40; mainly α - helices). Our results demonstrated that MoS2 monolayer has an exceptional capability to bind all peptides in a fast and strong manner. The strong attraction from the MoS2 nanosheet is more than enough to compensate the energy needed to unfold the peptide, regardless of the length, which induces drastic disruptions to the intra-peptide hydrogen bonds and subsequent secondary structures of α - helices. This universal phenomenon may point to the potential nanotoxicity of MoS2 when used in biological systems. Moreover, these results aligned well with previous findings on the potential cytotoxicity of TMD nanomaterials.