Gold nanorod and its impacting on latent membrane protein LMP1: A molecular dynamics approach

Abstract We report the impact of a PEGylated GNR on the structure of latent membrane protein 1 (LMP1) binding to tumor necrosis factor receptor (TNFR)-associated factor 3 (TRAF3) using molecular dynamics simulation. Focusing on the anisotropy of a GNR validated by experiment and finite-difference time-domain (FDTD) calculation, this study addressed three typical scenarios of LMP1-TRAF3 with a PEGylated GNR. The structure of LMP1-TRAF3 backbone, specifically the individual LMP1, changes with a PEGylated GNR included, and the variation is more significant along longitudinal axis than its transversal counterpart. Moreover, a heating-up GNR gains a more salient variation of LMP1 structure.