- Highly Ordered Self-Assembly of Native Proteins into 1D, 2D, and 3D Structures Modulated by the Tether Length of Assembly-Inducing Ligands
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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.
- Yang, Guang,Ding, Hong-Ming,Kochovski, Zdravko,Hu, Rongting,Lu, Yan,Ma, Yu-Qiang,Chen, Guosong,Jiang, Ming
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- An efficient and versatile approach for the preparation of a rhodamine B ester bioprobe library
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A general approach for the preparation of a library consisting of reactive rhodamine B (RhB) bioprobes based on ester or thioester linkages is described. The synthesis of this library proceeds fast and efficiently in one reaction step. Pure RhB ester chromophores are readily obtained directly from the reaction mixture following a simple and straight forward workup procedure without further HPLC purification required. A variety of functional groups are attached to the RhB scaffold yielding the functional chromophores in moderate to high yields with particular focus on introducing bioorthogonal substituents suitable for protein and peptide labeling. The approach reported herein provides a concise and practical route to access a variety of reactive RhB fluorophores that could be applied for various bioconjugation chemistries.
- Chen, Xi,Wu, Qianzhen,Henschke, Lars,Weber, Günther,Weil, Tanja
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- Aryloxymaleimides for cysteine modification, disulfide bridging and the dual functionalization of disulfide bonds
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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.
- Marculescu, Cristina,Kossen, Hanno,Morgan, Rachel E.,Mayer, Patrick,Fletcher, Sally A.,Tolner, Berend,Chester, Kerry A.,Jones, Lyn H.,Baker, James R.
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supporting information
p. 7139 - 7142
(2014/07/07)
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