Citation: Qi Qi, Zhao Tian-Xin, An Bo-Lin, Liu Xuan-Yong, Zhong Chao. Self-assembly and morphological characterization of two-component functional amyloid proteins[J]. Chinese Chemical Letters, ;2017, 28(5): 1062-1068. doi: 10.1016/j.cclet.2016.12.008 shu

Self-assembly and morphological characterization of two-component functional amyloid proteins

Qi Qi ^a,b,c ,
Zhao Tian-Xin ^a ,
An Bo-Lin ^a ,
Liu Xuan-Yong ^b ,
Zhong Chao ^a,,

a.
School of Physical Science and Technology, ShanghaiTech University, Shanghai 200120, China
b.
Shanghai Institute of Ceramics, Chinese Academy of Sciences, Shanghai 200050, China
c.
University of Chinese Academy of Sciences, Beijing 100049, China

Corresponding author: Zhong Chao, zhongchao@shanghaitech.edu.cn
Received Date: 8 October 2016
Revised Date: 10 November 2016
Accepted Date: 29 November 2016
Available Online: 10 May 2016

Figures(5)

Functional amyloid has been increasingly applied as self-assembling nanostructures to construct multifunctional biomaterials. However, little has been known how different side domains, varied fusion positions and subunits affect self-assembly and morphologies of amyloid fibrils. Here, we constructed three groups of two-component amyloid proteins based on CsgA, the major protein components of Escherichia coli biofilms, to bridge these gaps. We showed that all fusion proteins have amyloid features, as indicated by Congo red assay. Atomic force microscopy (AFM) indeed reveals that these fusion proteins are able to self-assemble into fibrils, with an average diameter of 0.5-2 nm and length of hundreds of nanometers to several micrometers. The diameter of fibrils increases with the increase of the molecular weight of fusion domains, while the dynamic assembly of recombinant proteins was delayed as a result of the introduction of fusion domains. Moreover, fusion of the same functional domains but at intermediate position seems to cause the most interference on fibril assembly compared with those fused at C or Nterminus, as mainly short and irregular fibrils were detected. This phenomenon appears more pronounced for randomly coiled mussel foot proteins (Mfps) than for rigid chitin-binding domain (CBD). Finally, increase of the molecular weight of tandem repeats in protein monomer seemed to increase the fibril diameter of the resultant fibrils, but either reduction of the tandem repeats of CsgA to one single belta-sheet loop or increase in the number of tandem repeats of CsgAs from one to four produced shorter and intermittent fibrils compared with CsgA control protein. These studies therefore provide insights into self-assembly of two-component amyloid proteins and lay the foundation for rational design of multifunctional molecular biomaterials.
- Amyloid,
- Biofilms,
- Atomic force microscopy,
- Self-assembly,
- Nanomaterials,
- Supramolecular structure
1. [1]
  Chiti F., Dobson C.M.. Protein misfolding, functional amyloid and human disease[J]. Annu. Rev. Biochem., 2006,75:333-366. doi: 10.1146/annurev.biochem.75.101304.123901
2. [2]
  Dobson C.M.. Protein folding and misfolding[J]. Nature, 2003,426:884-890. doi: 10.1038/nature02261
3. [3]
  Chapman M.R., Robinson L.S., Pinkner J.S.. Role of Escherichia coli curli operons in directing amyloid fiber formation[J]. Science, 2002,295:851-855. doi: 10.1126/science.1067484
4. [4]
  Fowler D.M., Koulov A.V., Alory-Jost C.. Functional amyloid formation within mammalian tissue[J]. PLoS Biol., 2006,4e6.
5. [5]
  Maji S.K., Perrin M.H., Sawaya M.R.. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules[J]. Science, 2009,325:328-332. doi: 10.1126/science.1173155
6. [6]
  Wu Z.F., Yang P.. Simple multipurpose surface functionalization by phase transited protein adhesion[J]. Adv. Mate. Interfaces, 2015,21400401. doi: 10.1002/admi.201400401
7. [7]
  Wang D.H., Ha Y., Gu J.. 2D protein supramolecular nanofilm with exceptionally large area and emergent functions[J]. Adv. Mater., 2016,28:7413-7423. doi: 10.1002/adma.201670239
8. [8]
  Gao A.T., Wu Q., Wang D.H.. A superhydrophobic surface templated by protein self-assembly and emerging application toward protein crystallization[J]. Adv. Mater., 2016,28:579-587. doi: 10.1002/adma.v28.3
9. [9]
  Zhong C., Gurry T., Cheng A.A.. Strong underwater adhesives made by self-assembling multi-protein nanofibres[J]. Nat. Nanotechnol., 2014,9:858-866. doi: 10.1038/nnano.2014.199
10. [10]
  Chen A.Y., Deng Z.T., Billings A.N.. Synthesis and patterning of tunable multiscale materials with engineered cells[J]. Nat. Mater., 2014,13:515-523. doi: 10.1038/nmat3912
11. [11]
  Nguyen P.Q., Botyanszki Z., Tay P.K., Joshi N.S.. Programmable biofilm-based materials from engineered curli nanofibres[J]. Nat. Commun., 2014,54945. doi: 10.1038/ncomms5945
12. [12]
  Blanco L.P., Evans M.L., Smith D.R., Badtke M.P., Chapman M.R.. Diversity, biogenesis and function of microbial amyloids[J]. Trends Microbiol., 2012,20:66-73. doi: 10.1016/j.tim.2011.11.005
13. [13]
  Barnhart M.M., Chapman M.R.. Curli biogenesis and function[J]. Annu. Rev. Microbiol., 2006,60:131-147. doi: 10.1146/annurev.micro.60.080805.142106
14. [14]
  Greenwald J., Riek R.. Biology of amyloid:structure, function, and regulation[J]. Structure, 2010,18:1244-1260. doi: 10.1016/j.str.2010.08.009
15. [15]
  Fowler D.M., Koulov A.V., Balch W.E., Kelly J.W.. Functional amyloid-from bacteria to humans[J]. Trends Biochem. Sci., 2007,32:217-224. doi: 10.1016/j.tibs.2007.03.003
16. [16]
  Zakeri B., Fierer J.O., Celik E.. Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin[J]. Proc. Natl. Acad. Sci. U. S. A., 2012,109:E690-E697. doi: 10.1073/pnas.1115485109
17. [17]
  Ikegami T., Okada T., Hashimoto M.. Solution structure of the chitinbinding domain of Bacillus circulans WL-12 chitinase A1[J]. J. Biol. Chem., 2000,275:13654-13661. doi: 10.1074/jbc.275.18.13654
18. [18]
  Hickey C.M., Wilson N.R., Hochstrasser M.. Function and regulation of SUMO proteases[J]. Nat. Rev. Mol. Cell Biol., 2012,13:755-766. doi: 10.1038/nrm3478
19. [19]
  Sambashivan S., Liu Y.S., Sawaya M.R., Mari G., David E.. Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure[J]. Nature, 2005,437:266-269. doi: 10.1038/nature03916
20. [20]
  Hwang D.S., Waite J.H.. Three intrinsically unstructured mussel adhesive proteins, mfp-1, mfp-2, and mfp-3:analysis by circular dichroism[J]. Protein Sci., 2012,21:1689-1695. doi: 10.1002/pro.v21.11
21. [21]
  Collinson S.K., Parker J.M.R., Hodges R.S., Kay W.W.. Structural predictions of AgfA, the insoluble fimbrial subunit of salmonella thin aggregative fimbriae[J]. J. Mol. Biol., 1999,290:741-756. doi: 10.1006/jmbi.1999.2882
22. [22]
  Tian P.F., Boomsma W., Wang Y.. Structure of a functional amyloid protein subunit computed using sequence variation[J]. J. Am. Chem. Soc., 2015,137:22-25. doi: 10.1021/ja5093634
23. [23]
  Wang X., Smith D.R., Jones J.W., Chapman M.R.. In vitro polymerization of a functional Escherichia coli amyloid protein[J]. J. Biol. Chem., 2007,282:3713-3719.
24. [24]
  Knowles T.P.J., Buehler M.J.. Nanomechanics of functional and pathological amyloid materials[J]. Nat. Nanotechnol., 2011,6:469-479. doi: 10.1038/nnano.2011.102
25. [25]
  Knowles T.P.J., Waudby C.A., Devlin G.L.. An analytical solution to the kinetics of breakable filament assembly[J]. Science, 2009,326:1533-1537. doi: 10.1126/science.1178250
26. [26]
  Relini A., Torrassa S., Ferrando R.. Detection of populations of amyloidlike protofibrils with different physical properties[J]. Biophys. J., 2010,98:1277-1284. doi: 10.1016/j.bpj.2009.11.052
1. [1]
  Shengyong Liu , Hui Li , Wei Zhang , Yan Zhang , Yan Dong , Wei Tian . Multiple host-guest and metal coordination interactions induce supramolecular assembly and structural transition. Chinese Chemical Letters, 2025, 36(6): 110465-. doi: 10.1016/j.cclet.2024.110465
2. [2]
  Yuanpeng Ye , Longfei Yao , Guofeng Liu . Engineering circularly polarized luminescence through symmetry manipulation in achiral tetraphenylpyrazine structures. Chinese Journal of Structural Chemistry, 2025, 44(2): 100460-100460. doi: 10.1016/j.cjsc.2024.100460
3. [3]
  Sifan Du , Yuan Wang , Fulin Wang , Tianyu Wang , Li Zhang , Minghua Liu . Evolution of hollow nanosphere to microtube in the self-assembly of chiral dansyl derivatives and inversed circularly polarized luminescence. Chinese Chemical Letters, 2024, 35(7): 109256-. doi: 10.1016/j.cclet.2023.109256
4. [4]
  Hao Zhang , Hao Liu , Ke Huang , Qingxiu Xia , Hongjie Xiong , Xiaohui Liu , Hui Jiang , Xuemei Wang . Ionic exchange based intracellular self-assembly of pitaya-structured nanoparticles for tumor imaging. Chinese Chemical Letters, 2025, 36(6): 110281-. doi: 10.1016/j.cclet.2024.110281
5. [5]
  Xuanyu Wang , Zhao Gao , Wei Tian . Supramolecular confinement effect enabling light-harvesting system for photocatalytic α-oxyamination reaction. Chinese Chemical Letters, 2024, 35(11): 109757-. doi: 10.1016/j.cclet.2024.109757
6. [6]
  Yuwen Zhu , Xiang Deng , Yan Wu , Baode Shen , Lingyu Hang , Yuye Xue , Hailong Yuan . Formation mechanism of herpetrione self-assembled nanoparticles based on pH-driven method. Chinese Chemical Letters, 2025, 36(1): 109733-. doi: 10.1016/j.cclet.2024.109733
7. [7]
  Miao-Miao Chen , Min-Ling Zhang , Xiao Song , Jun Jiang , Xiaoqian Tang , Qi Zhang , Xiuhua Zhang , Peiwu Li . Smartphone-assisted electrochemiluminescence imaging test strips towards dual-signal visualized and sensitive monitoring of aflatoxin B1 in corn samples. Chinese Chemical Letters, 2025, 36(1): 109785-. doi: 10.1016/j.cclet.2024.109785
8. [8]
  Xu Luo , Jinwen Xiao , Qiming Yang , Xiaolong Lu , Qianjun Huang , Xiaojun Ai , Bo Li , Li Sun , Long Chen . Biomaterials for surgical repair of osteoporotic bone defects. Chinese Chemical Letters, 2025, 36(1): 109684-. doi: 10.1016/j.cclet.2024.109684
9. [9]
  Jingqi Xin , Shupeng Han , Meichen Zheng , Chenfeng Xu , Zhongxi Huang , Bin Wang , Changmin Yu , Feifei An , Yu Ren . A nitroreductase-responsive nanoprobe with homogeneous composition and high loading for preoperative non-invasive tumor imaging and intraoperative guidance. Chinese Chemical Letters, 2024, 35(7): 109165-. doi: 10.1016/j.cclet.2023.109165
10. [10]
  Keyang Li , Yanan Wang , Yatao Xu , Guohua Shi , Sixian Wei , Xue Zhang , Baomei Zhang , Qiang Jia , Huanhua Xu , Liangmin Yu , Jun Wu , Zhiyu He . Flash nanocomplexation (FNC): A new microvolume mixing method for nanomedicine formulation. Chinese Chemical Letters, 2024, 35(10): 109511-. doi: 10.1016/j.cclet.2024.109511
11. [11]
  Xian Yan , Huawei Xie , Gao Wu , Fang-Xing Xiao . Boosted solar water oxidation steered by atomically precise alloy nanocluster. Chinese Chemical Letters, 2025, 36(1): 110279-. doi: 10.1016/j.cclet.2024.110279
12. [12]
  Feng Cao , Chunxiang Xian , Tianqi Yang , Yue Zhang , Haifeng Chen , Xinping He , Xukun Qian , Shenghui Shen , Yang Xia , Wenkui Zhang , Xinhui Xia . Gelation-pyrolysis strategy for fabrication of advanced carbon/sulfur cathodes for lithium-sulfur batteries. Chinese Chemical Letters, 2025, 36(3): 110575-. doi: 10.1016/j.cclet.2024.110575
13. [13]
  Fengying Ye , Ming Hu , Jun Luo , Wei Yu , Zhirong Xu , Jinjin Fu , Yansong Zheng . Significantly boosting circularly polarized luminescence by synergy of helical and planar chirality. Chinese Chemical Letters, 2025, 36(5): 110724-. doi: 10.1016/j.cclet.2024.110724
14. [14]
  Weibin Shen , Jie Liu , Gongyu Wen , Shuai Li , Binhui Yu , Shuangyu Song , Bojie Gong , Rongyang Zhang , Shibao Liu , Hongpeng Wang , Yao Wang , Yujing Liu , Huadong Yuan , Jianming Luo , Shihui Zou , Xinyong Tao , Jianwei Nai . Formation of FeNi-based nanowire-assembled superstructures with tunable anions for electrocatalytic oxygen evolution reaction. Chinese Chemical Letters, 2025, 36(7): 110184-. doi: 10.1016/j.cclet.2024.110184
15. [15]
  Changhui Yu , Peng Shang , Huihui Hu , Yuening Zhang , Xujin Qin , Linyu Han , Caihe Liu , Xiaohan Liu , Minghua Liu , Yuan Guo , Zhen Zhang . Evolution of template-assisted two-dimensional porphyrin chiral grating structure by directed self-assembly using chiral second harmonic generation microscopy. Chinese Chemical Letters, 2024, 35(10): 109805-. doi: 10.1016/j.cclet.2024.109805
16. [16]
  Zhenzhu Wang , Chenglong Liu , Yunpeng Ge , Wencan Li , Chenyang Zhang , Bing Yang , Shizhong Mao , Zeyuan Dong . Differentiated self-assembly through orthogonal noncovalent interactions towards the synthesis of two-dimensional woven supramolecular polymers. Chinese Chemical Letters, 2024, 35(5): 109127-. doi: 10.1016/j.cclet.2023.109127
17. [17]
  Zunyuan Xie , Lijin Yang , Zixiao Wan , Xiaoyu Liu , Yushan He . Exploration of the Preparation and Characterization of Nano Barium Titanate and Its Application in Inorganic Chemistry Laboratory Teaching. University Chemistry, 2024, 39(4): 62-69. doi: 10.3866/PKU.DXHX202310137
18. [18]
  Simin Fang , Wei Huang , Guanghua Yu , Cong Wei , Mingli Gao , Guangshui Li , Hongjun Tian , Wan Li . Integrating Science and Education in a Comprehensive Chemistry Design Experiment: The Preparation of Copper(I) Oxide Nanoparticles and Its Application in Dye Water Remediation. University Chemistry, 2024, 39(8): 282-289. doi: 10.3866/PKU.DXHX202401023
19. [19]
  Yihao Zhang , Yang Jiao , Xianchao Jia , Qiaojia Guo , Chunying Duan . Highly effective self-assembled porphyrin MOCs nanomaterials for enhanced photodynamic therapy in tumor. Chinese Chemical Letters, 2024, 35(5): 108748-. doi: 10.1016/j.cclet.2023.108748
20. [20]
  Xingwen Cheng , Haoran Ren , Jiangshan Luo . Boosting the self-trapped exciton emission in vacancy-ordered double perovskites via supramolecular assembly. Chinese Journal of Structural Chemistry, 2024, 43(6): 100306-100306. doi: 10.1016/j.cjsc.2024.100306

Get Citation

PDF

XML

Metrics

PDF Downloads(3)
Abstract views(959)
HTML views(36)

通讯作者: 陈斌, bchen63@163.com

1.
沈阳化工大学材料科学与工程学院沈阳 110142