Protein microtubule is a significant self-assembled architecture found in nature with crucial biological functions. However, mimicking protein microtubules with precise structure and controllable self-assembly behavior remains highly challenging. In this work, we demonstrate that by using dual supramolecular interactions from a series of well-designed ligands, i.e., protein-sugar interaction and pi-pi stacking, highly homogeneous protein microtubes were achieved from tetrameric soybean agglutinin without any chemical or biological modification. Using combined cryo-EM single-particle reconstruction and computational modeling, the accurate structure of protein microtube was determined. The helical protein microtube is consisted of three protofilaments, each of which features an array of soybean agglutinin tetramer linked by the designed ligands. Notably, the microtubes resemble the natural microtubules in their structural and dynamic features such as the shape and diameter and the controllable and reversible assembly behavior, among others. Furthermore, the protein microtubes showed an ability to enhance immune response, demonstrating its great potential for biological applications.
[1]Fudan Univ, State Key Lab Mol Engn Polymers, Shanghai 200433, Peoples R China.
[2]Fudan Univ, Dept Macromol Sci, Shanghai 200433, Peoples R China.
[3]Helmholtz Zentrum Berlin Mat & Energie, Soft Matter & Funct Mat, D-14109 Berlin, Germany.
[4]Chinese Acad Sci, Shanghai Inst Organ Chem, Interdisciplinary Res Ctr Biol & Chem, Shanghai 200032, Peoples R China.
[5]Humboldt Univ, Inst Phys, TEM Grp, D-12489 Berlin, Germany.
[6]Univ Calif Los Angeles, David Geffen Sch Med, Easton Ctr Alzheimers Dis Res, Dept Neurol, Los Angeles, CA 90095 USA.
[7]Tsinghua Univ, Tsinghua Peking Joint Ctr Life Sci, Struct Biol Ctr, Sch Life Sci,Key Lab Prot Sci,Minist Educ, Beijing 100084, Peoples R China.
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