1033001-11-4Relevant articles and documents
Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
Yang, Guang,Ding, Hong-Ming,Kochovski, Zdravko,Hu, Rongting,Lu, Yan,Ma, Yu-Qiang,Chen, Guosong,Jiang, Ming
, p. 10691 - 10695 (2017)
In nature, proteins self-assemble into various structures with different dimensions. To construct these nanostructures in laboratories, normally proteins with different symmetries are selected. However, most of these approaches are engineering-intensive and highly dependent on the accuracy of the protein design. Herein, we report that a simple native protein LecA assembles into one-dimensional nanoribbons and nanowires, two-dimensional nanosheets, and three-dimensional layered structures controlled mainly by small-molecule assembly-inducing ligands RnG (n=1, 2, 3, 4, 5) with varying numbers of ethylene oxide repeating units. To understand the formation mechanism of the different morphologies controlled by the small-molecule structure, molecular simulations were performed from microscopic and mesoscopic view, which presented a clear relationship between the molecular structure of the ligands and the assembled patterns. These results introduce an easy strategy to control the assembly structure and dimension, which could shed light on controlled protein assembly.
Aryloxymaleimides for cysteine modification, disulfide bridging and the dual functionalization of disulfide bonds
Marculescu, Cristina,Kossen, Hanno,Morgan, Rachel E.,Mayer, Patrick,Fletcher, Sally A.,Tolner, Berend,Chester, Kerry A.,Jones, Lyn H.,Baker, James R.
supporting information, p. 7139 - 7142 (2014/07/07)
Tuning the properties of maleimide reagents holds significant promise in expanding the toolbox of available methods for bioconjugation. Herein we describe aryloxymaleimides which represent 'next generation maleimides' of attenuated reactivity, and demonstrate their ability to enable new methods for protein modification at disulfide bonds.