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Journal articles on the topic 'Proteins self-assembly'

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Author: Grafiati

Published: 10 March 2023

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1

van der Linden, Erik, and Paul Venema. "Self-assembly and aggregation of proteins." Current Opinion in Colloid & Interface Science 12, no. 4-5 (October 2007): 158–65. http://dx.doi.org/10.1016/j.cocis.2007.07.010.

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2

Ringler, P. "Self-Assembly of Proteins into Designed Networks." Science 302, no. 5642 (October 3, 2003): 106–9. http://dx.doi.org/10.1126/science.1088074.

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3

Rad, Behzad, Tom Haxton, Seong-Ho Shin, Steve Whitelam, and Caroline Ajo-Franklin. "Self Assembly Pathways of Surface-Layer Proteins." Biophysical Journal 102, no. 3 (January 2012): 261a. http://dx.doi.org/10.1016/j.bpj.2011.11.1437.

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4

Yang, Liulin, Aijie Liu, Shuqin Cao, Rindia M. Putri, Pascal Jonkheijm, and Jeroen J. L. M. Cornelissen. "Self-Assembly of Proteins: Towards Supramolecular Materials." Chemistry - A European Journal 22, no. 44 (August 18, 2016): 15570–82. http://dx.doi.org/10.1002/chem.201601943.

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5

Ren, Huan, Lifang Wu, Lina Tan, Yanni Bao, Yuchen Ma, Yong Jin, and Qianli Zou. "Self-assembly of amino acids toward functional biomaterials." Beilstein Journal of Nanotechnology 12 (October 12, 2021): 1140–50. http://dx.doi.org/10.3762/bjnano.12.85.

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Biomolecules, such as proteins and peptides, can be self-assembled. They are widely distributed, easy to obtain, and biocompatible. However, the self-assembly of proteins and peptides has disadvantages, such as difficulty in obtaining high quantities of materials, high cost, polydispersity, and purification limitations. The difficulties in using proteins and peptides as functional materials make it more complicate to arrange assembled nanostructures at both microscopic and macroscopic scales. Amino acids, as the smallest constituent of proteins and the smallest constituent in the bottom-up approach, are the smallest building blocks that can be self-assembled. The self-assembly of single amino acids has the advantages of low synthesis cost, simple modeling, excellent biocompatibility and biodegradability in vivo. In addition, amino acids can be assembled with other components to meet multiple scientific needs. However, using these simple building blocks to design attractive materials remains a challenge due to the simplicity of the amino acids. Most of the review articles about self-assembly focus on large molecules, such as peptides and proteins. The preparation of complicated materials by self-assembly of amino acids has not yet been evaluated. Therefore, it is of great significance to systematically summarize the literature of amino acid self-assembly. This article reviews the recent advances in amino acid self-assembly regarding amino acid self-assembly, functional amino acid self-assembly, amino acid coordination self-assembly, and amino acid regulatory functional molecule self-assembly.

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6

Henson, Brandon W., Edward M. Perkins, Jonathan E. Cothran, and Prashant Desai. "Self-Assembly of Epstein-Barr Virus Capsids." Journal of Virology 83, no. 8 (January 21, 2009): 3877–90. http://dx.doi.org/10.1128/jvi.01733-08.

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ABSTRACT Epstein-Barr virus (EBV), a member of the Gammaherpesvirus family, primarily infects B lymphocytes and is responsible for a number of lymphoproliferative diseases. The molecular genetics of the assembly pathway and high-resolution structural analysis of the capsid have not been determined for this lymphocryptovirus. As a first step in studying EBV capsid assembly, the baculovirus expression vector (BEV) system was used to express the capsid shell proteins BcLF1 (major capsid protein), BORF1 (triplex protein), BDLF1 (triplex protein), and BFRF3 (small capsid protein); the internal scaffold protein, BdRF1; and the maturational protease (BVRF2). Coinfection of insect cells with the six viruses expressing these proteins resulted in the production of closed capsid structures as judged by electron microscopy and sedimentation methods. Therefore, as shown for other herpesviruses, only six proteins are required for EBV capsid assembly. Furthermore, the small capsid protein of EBV (BFRF3), like that of Kaposi's sarcoma-associated herpesvirus, was found to be required for assembly of a stable structure. Localization of the small capsid protein to nuclear assembly sites required both the major capsid (BcLF1) and scaffold proteins (BdRF1) but not the triplex proteins. Mutational analysis of BFRF3 showed that the N-terminal half (amino acids 1 to 88) of this polypeptide is required and sufficient for capsid assembly. A region spanning amino acids 65 to 88 is required for the concentration of BFRF3 at a subnuclear site and the N-terminal 65 amino acids contain the sequences required for interaction with major capsid protein. These studies have identified the multifunctional role of the gammaherpesvirus small capsid proteins.

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7

Wołek, Karol, and Marek Cieplak. "Self-assembly of model proteins into virus capsids." Journal of Physics: Condensed Matter 29, no. 47 (November 7, 2017): 474003. http://dx.doi.org/10.1088/1361-648x/aa9351.

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8

Javid, Nadeem, Sangita Roy, Mischa Zelzer, Zhimou Yang, Jan Sefcik, and Rein V. Ulijn. "Cooperative Self-Assembly of Peptide Gelators and Proteins." Biomacromolecules 14, no. 12 (November 27, 2013): 4368–76. http://dx.doi.org/10.1021/bm401319c.

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9

Pengelly, Kate, Ana Loncar, Alex A. Perieteanu, and John F. Dawson. "Cysteine engineering of actin self-assembly interfaces." Biochemistry and Cell Biology 87, no. 4 (August 2009): 663–75. http://dx.doi.org/10.1139/o09-012.

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The Holmes model of filamentous actin (F-actin) and recent structural studies suggest specific atomic interactions between F-actin subunits. We tested these interactions through a cysteine-engineering approach with the goal of inhibiting filament formation by introducing chemical groups at sites important for polymerization. We substituted surface amino acids on the actin molecule with cysteine residues and tested the effect of producing these actin mutant proteins in a yeast expression system. The intrinsic folding and polymerization characteristics of the cysteine-engineered actin proteins were measured. The effect of chemical modification of the introduced cysteine residues on the polymerization of the actin mutant proteins was also examined. Modification of cysteine residues with large hydrophobic reagents resulted in polymerization inhibition. We examined the finding that the D288C actin protein does not polymerize under oxidizing conditions and forms protein aggregates when magnesium and EGTA are present. Chemical crosslinking experiments revealed the presence of a lower dimer when only D288C actin was present. When both D288C and A204C actin were present, crosslinking experiments support the proximity of Asp288 on the barbed end of one subunit to Ala204 on the pointed end of a neighboring subunit in the Holmes model of F-actin.

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10

Garcia-Seisdedos, Hector, Charly Empereur-Mot, Nadav Elad, and Emmanuel D. Levy. "Proteins evolve on the edge of supramolecular self-assembly." Nature 548, no. 7666 (August 2, 2017): 244–47. http://dx.doi.org/10.1038/nature23320.

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11

Park, Won Min, and Julie A. Champion. "Thermally Triggered Self-Assembly of Folded Proteins into Vesicles." Journal of the American Chemical Society 136, no. 52 (December 11, 2014): 17906–9. http://dx.doi.org/10.1021/ja5090157.

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12

Knowles, Tuomas P. J., Tomas W. Oppenheim, Alexander K. Buell, Dimitri Y. Chirgadze, and Mark E. Welland. "Nanostructured films from hierarchical self-assembly of amyloidogenic proteins." Nature Nanotechnology 5, no. 3 (February 28, 2010): 204–7. http://dx.doi.org/10.1038/nnano.2010.26.

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13

James, Susan, Michelle K. Quinn, and Jennifer J. McManus. "The self assembly of proteins; probing patchy protein interactions." Physical Chemistry Chemical Physics 17, no. 7 (2015): 5413–20. http://dx.doi.org/10.1039/c4cp05892e.

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Anisotropy is central to protein self-assembly. The kinetic and thermodynamic properties of proteins in which competing interactions exist due to the anisotropic or patchy nature of the protein surface have been explored using a phase diagram approach.

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14

Kwiecinski, James, S. Jonathan Chapman, and Alain Goriely. "Self-assembly of a filament by curvature-inducing proteins." Physica D: Nonlinear Phenomena 344 (April 2017): 68–80. http://dx.doi.org/10.1016/j.physd.2016.12.001.

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15

Garcia Seisdedos, Héctor. "Proteins Evolve on the Edge of Supramolecular Self-Assembly." Biophysical Journal 112, no. 3 (February 2017): 200a. http://dx.doi.org/10.1016/j.bpj.2016.11.1107.

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16

Park, Jin-Seung, Ji-Young Ahn, Sung-Hyun Lee, Hyewon Lee, Kyung-Yeon Han, Hyuk-Seong Seo, Keum-Young Ahn, et al. "Enhanced stability of heterologous proteins by supramolecular self-assembly." Applied Microbiology and Biotechnology 75, no. 2 (February 14, 2007): 347–55. http://dx.doi.org/10.1007/s00253-006-0826-3.

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17

Cartwright, Julyan H. E., and Antonio G. Checa. "The dynamics of nacre self-assembly." Journal of The Royal Society Interface 4, no. 14 (December 8, 2006): 491–504. http://dx.doi.org/10.1098/rsif.2006.0188.

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We show how nacre and pearl construction in bivalve and gastropod molluscs can be understood in terms of successive processes of controlled self-assembly from the molecular- to the macro-scale. This dynamics involves the physics of the formation of both solid and liquid crystals and of membranes and fluids to produce a nanostructured hierarchically constructed biological composite of polysaccharides, proteins and mineral, whose mechanical properties far surpass those of its component parts.

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18

Rode, Sebastian, Jens Elgeti, and Gerhard Gompper. "Chiral-filament self-assembly on curved manifolds." Soft Matter 16, no. 46 (2020): 10548–57. http://dx.doi.org/10.1039/d0sm01339k.

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Chiral proteins can assemble as twisted ribbons on curved surfaces. Simulations of anisotropic building blocks on a cylindrical surface show a helical assembly with a preferred helix angle, and a power-law growth of the filament length in time.

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19

Schaefer, Charley, René A. J. de Bruijn, and Tom C. B. McLeish. "Ligand-regulated oligomerisation of allosterically interacting proteins." Soft Matter 14, no. 34 (2018): 6961–68. http://dx.doi.org/10.1039/c8sm00943k.

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20

Clark, John I. "Self-assembly of protein aggregates in ageing disorders: the lens and cataract model." Philosophical Transactions of the Royal Society B: Biological Sciences 368, no. 1617 (May 5, 2013): 20120104. http://dx.doi.org/10.1098/rstb.2012.0104.

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Cataract, neurodegenerative disease, macular degeneration and pathologies of ageing are often characterized by the slow progressive destabilization of proteins and their self-assembly to amyloid-like fibrils and aggregates. During normal cell differentiation, protein self-assembly is well established as a dynamic mechanism for cytoskeletal organization. With the increased emphasis on ageing disorders, there is renewed interest in small-molecule regulators of protein self-assembly. Synthetic peptides, mini-chaperones, aptamers, ATP and pantethine reportedly regulate self-assembly mechanisms involving small stress proteins, represented by human αB-crystallin, and their targets. Small molecules are being considered for direct application as molecular therapeutics to protect against amyloid and protein aggregation disorders in ageing cells and tissues in vivo . The identification of specific interactive peptide sites for effective regulation of protein self-assembly is underway using conventional and innovative technologies. The quantification of the functional interactions between small stress proteins and their targets in vivo remains a top research priority. The quantitative parameters controlling protein–protein interactions in vivo need characterization to understand the fundamental biology of self-assembling systems in normal cells and disorders of ageing.

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21

Liu, Xiaosong, Fan Zheng, A. Jürgensen, V. Perez-Dieste, D. Y. Petrovykh, N. L. Abbott, and F. J. Himpsel. "Self-assembly of biomolecules at surfaces characterized by NEXAFS." Canadian Journal of Chemistry 85, no. 10 (October 1, 2007): 793–800. http://dx.doi.org/10.1139/v07-079.

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Surface science has made great strides towards tailoring surface properties via self-assembly of nanoscale molecular adsorbates. It is now possible to functionalize surfaces with complex biomolecules such as DNA and proteins. This brief overview shows how NEXAFS (near edge X-ray absorption fine structure spectroscopy) can be used to characterize the assembly of biological molecules at surfaces in atom- and orbital-specific fashion. To illustrate the range of applications, we begin with simple self-assembled monolayers (SAMs), proceed to SAMs with customized terminal groups, and finish with DNA oligonucleotides and Ribonuclease A, a small protein containing 124 amino acids. The N 1s absorption edge is particularly useful for characterizing DNA and proteins because it selectively interrogates the π* orbitals in nucleobases and the peptide bonds in proteins. Information about the orientation of molecular orbitals is obtained from the polarization dependence. Quantitative NEXAFS models explain the polarization dependence in terms of molecular orientation and structure.Key words: NEXAFS, bio-interfaces, ribonuclease A, immobilization, orientation.

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22

Thirumalai, D. "Universal relations in the self-assembly of proteins and RNA." Physical Biology 11, no. 5 (October 8, 2014): 053005. http://dx.doi.org/10.1088/1478-3975/11/5/053005.

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23

Varjonen, Suvi, Päivi Laaksonen, Arja Paananen, Hanna Valo, Hendrik Hähl, Timo Laaksonen, and Markus Ben Linder. "Self-assembly of cellulose nanofibrils by genetically engineered fusion proteins." Soft Matter 7, no. 6 (2011): 2402. http://dx.doi.org/10.1039/c0sm01114b.

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24

Nitsche, Christoph, Mithun C. Mahawaththa, Walter Becker, Thomas Huber, and Gottfried Otting. "Site-selective tagging of proteins by pnictogen-mediated self-assembly." Chemical Communications 53, no. 79 (2017): 10894–97. http://dx.doi.org/10.1039/c7cc06155b.

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25

Zhang, Minmin, Shuqin Cao, Aijie Liu, Jeroen J. L. M. Cornelissen, and Serge G. Lemay. "Self-Assembly of Viral Capsid Proteins Driven by Compressible Nanobubbles." Journal of Physical Chemistry Letters 11, no. 24 (December 3, 2020): 10421–24. http://dx.doi.org/10.1021/acs.jpclett.0c02658.

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26

Stephanopoulos, Nicholas. "Hybrid Nanostructures from the Self-Assembly of Proteins and DNA." Chem 6, no. 2 (February 2020): 364–405. http://dx.doi.org/10.1016/j.chempr.2020.01.012.

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27

Maria Herrera, Ana, Anil K. Dasanna, and Frauke Gräter. "Towards Simulating Large-Scale Self-Assembly of Proteins under Flow." Biophysical Journal 112, no. 3 (February 2017): 592a—593a. http://dx.doi.org/10.1016/j.bpj.2016.11.3188.

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28

Schneider, Anna R., and Phillip L. Geissler. "Simulated Self-Assembly of Photosynthesis Proteins in Stacked Thylakoid Membranes." Biophysical Journal 98, no. 3 (January 2010): 174a. http://dx.doi.org/10.1016/j.bpj.2009.12.937.

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29

RICKMAN, Colin, Kuang HU, Joe CARROLL, and Bazbek DAVLETOV. "Self-assembly of SNARE fusion proteins into star-shaped oligomers." Biochemical Journal 388, no. 1 (May 10, 2005): 75–79. http://dx.doi.org/10.1042/bj20041818.

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Three evolutionarily conserved proteins known as SNAREs (soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors) mediate exocytosis from single cell eukaryotes to neurons. Among neuronal SNAREs, syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa) reside on the plasma membrane, whereas synaptobrevin resides on synaptic vesicles prior to fusion. The SNARE motifs of the three proteins form a helical bundle which probably drives membrane fusion. Since studies in vivo suggested an importance for multiple SNARE complexes in the fusion process, and models appeared in the literature with large numbers of SNARE bundles executing the fusion process, we analysed the quaternary structure of the full-length native SNARE complexes in detail. By employing a preparative immunoaffinity procedure we isolated all of the SNARE complexes from brain, and have shown by size-exclusion chromatography and negative stain electron microscopy that they exist as approx. 30 nm particles containing, most frequently, 3 or 4 bundles emanating from their centre. Using highly purified, individual, full-length SNAREs we demonstrated that the oligomerization of SNAREs into star-shaped particles with 3 to 4 bundles is an intrinsic property of these proteins and is not dependent on other proteins, as previously hypothesized. The average number of the SNARE bundles in the isolated fusion particles corresponds well with the co-operativity observed in calcium-triggered neuronal exocytosis.

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30

Yewdall, N. Amy, Timothy M. Allison, F. Grant Pearce, Carol V. Robinson, and Juliet A. Gerrard. "Self-assembly of toroidal proteins explored using native mass spectrometry." Chemical Science 9, no. 28 (2018): 6099–106. http://dx.doi.org/10.1039/c8sc01379a.

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The peroxiredoxins are a well characterised family of toroidal proteins which can self-assemble into a striking array of quaternary structures, including protein nanotubes, making them attractive as building blocks for nanotechnology.

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31

Zhu, Kui, Jianzhong Shen, Richard Dietrich, Andrea Didier, Xingyu Jiang, and Erwin Märtlbauer. "Ordered self-assembly of proteins for computation in mammalian cells." Chem. Commun. 50, no. 6 (2014): 676–78. http://dx.doi.org/10.1039/c3cc48100j.

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32

Martinez-Avila, Olga M., Shenping Wu, Yifan Cheng, Robert Lee, Feroz Khan, and Stefan Habelitz. "Self-assembly of amelogenin proteins at the water-oil interface." European Journal of Oral Sciences 119 (December 2011): 75–82. http://dx.doi.org/10.1111/j.1600-0722.2011.00907.x.

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33

Yu, Shaoyong, Ping Yao, Ming Jiang, and Guangzhao Zhang. "Nanogels prepared by self-assembly of oppositely charged globular proteins." Biopolymers 83, no. 2 (October 5, 2006): 148–58. http://dx.doi.org/10.1002/bip.20539.

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34

Cruz-Chu, Eduardo R., Konstantinos Gkagkas, and Frauke Graeter. "Self Assembly of Disordered Folded Multiphase Proteins by Computer Simulations." Biophysical Journal 110, no. 3 (February 2016): 323a. http://dx.doi.org/10.1016/j.bpj.2015.11.1736.

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35

Liao, Xinyu, and Prashant K. Purohit. "Kinetics of self-assembly of inclusions due to lipid membrane thickness interactions." Soft Matter 17, no. 9 (2021): 2539–56. http://dx.doi.org/10.1039/d0sm01752c.

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36

Grinkova, Y. V., I. G. Denisov, and S. G. Sligar. "Engineering extended membrane scaffold proteins for self-assembly of soluble nanoscale lipid bilayers." Protein Engineering Design and Selection 23, no. 11 (September 3, 2010): 843–48. http://dx.doi.org/10.1093/protein/gzq060.

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37

Ching, G. Y., and R. K. Liem. "Analysis of the roles of the head domains of type IV rat neuronal intermediate filament proteins in filament assembly using domain-swapped chimeric proteins." Journal of Cell Science 112, no. 13 (July 1, 1999): 2233–40. http://dx.doi.org/10.1242/jcs.112.13.2233.

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Type IV neuronal intermediate filament proteins consist of alpha-internexin, which can self-assemble into filaments and the neurofilament triplet proteins, which are obligate heteropolymers, at least in rodents. These IF proteins therefore provide good systems for elucidating the mechanism of intermediate filament assembly. To analyze the roles of the head domains of these proteins in contributing to their differential assembly properties, we generated chimeric proteins by swapping the head domains between rat alpha-internexin and either rat NF-L or NF-M and examined their assembly properties in transfected cells that lack their own cytoplasmic intermediate filament network. Lalphaalpha and Malphaalpha, the chimeric proteins generated by replacing the head domain of alpha-internexin with those of NF-L and NF-M, respectively, were unable to self-assemble into filaments. In contrast, alphaLL, a chimeric NF-L protein generated by replacing the head domain of NF-L with that of alpha-internexin, was able to self-assemble into filaments, whereas MLL, a chimeric NF-L protein containing the NF-M head domain, was unable to do so. These results demonstrate that the alpha-internexin head domain is essential for alpha-internexin's ability to self-assemble. While coassembly of Lalphaalpha with NF-M and coassembly of Malphaalpha with NF-L resulted in formation of filaments, coassembly of Lalphaalpha with NF-L and coassembly of Malphaalpha with NF-M yielded punctate patterns. These coassembly results show that heteropolymeric filament formation requires that one partner has the NF-L head domain and the other partner has the NF-M head domain. Thus, the head domains of rat NF-L and NF-M play important roles in determining the obligate heteropolymeric nature of filament formation. The data obtained from these self-assembly and coassembly studies provide some new insights into the mechanism of intermediate filament assembly.

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38

Bromley, Keith M., Ryan J. Morris, Laura Hobley, Giovanni Brandani, Rachel M. C. Gillespie, Matthew McCluskey, Ulrich Zachariae, Davide Marenduzzo, Nicola R. Stanley-Wall, and Cait E. MacPhee. "Interfacial self-assembly of a bacterial hydrophobin." Proceedings of the National Academy of Sciences 112, no. 17 (April 13, 2015): 5419–24. http://dx.doi.org/10.1073/pnas.1419016112.

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The majority of bacteria in the natural environment live within the confines of a biofilm. The Gram-positive bacterium Bacillus subtilis forms biofilms that exhibit a characteristic wrinkled morphology and a highly hydrophobic surface. A critical component in generating these properties is the protein BslA, which forms a coat across the surface of the sessile community. We recently reported the structure of BslA, and noted the presence of a large surface-exposed hydrophobic patch. Such surface patches are also observed in the class of surface-active proteins known as hydrophobins, and are thought to mediate their interfacial activity. However, although functionally related to the hydrophobins, BslA shares no sequence nor structural similarity, and here we show that the mechanism of action is also distinct. Specifically, our results suggest that the amino acids making up the large, surface-exposed hydrophobic cap in the crystal structure are shielded in aqueous solution by adopting a random coil conformation, enabling the protein to be soluble and monomeric. At an interface, these cap residues refold, inserting the hydrophobic side chains into the air or oil phase and forming a three-stranded β-sheet. This form then self-assembles into a well-ordered 2D rectangular lattice that stabilizes the interface. By replacing a hydrophobic leucine in the center of the cap with a positively charged lysine, we changed the energetics of adsorption and disrupted the formation of the 2D lattice. This limited structural metamorphosis represents a previously unidentified environmentally responsive mechanism for interfacial stabilization by proteins.

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39

Li, Jie, Linlin Zhang, Yang Liu, Jing Wen, Di Wu, Duo Xu, Tatiana Segura, Jing Jin, Yunfeng Lu, and Hui Wang. "An intracellular protein delivery platform based on glutathione-responsive protein nanocapsules." Chemical Communications 52, no. 93 (2016): 13608–11. http://dx.doi.org/10.1039/c6cc05099a.

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We reported an efficient strategy for the intracellular delivery of proteins based on assembling proteins with a self-crosslinkable polymer. The disulfide-crosslinking structure enhances the stability of the protein–polymer assembly, and also allows effective dissociation of the assembly in response to glutathione.

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40

Aldana, Maximino, Miguel Fuentes-Cabrera, and Martín Zumaya. "Self-Propulsion Enhances Polymerization." Entropy 22, no. 2 (February 22, 2020): 251. http://dx.doi.org/10.3390/e22020251.

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Self-assembly is a spontaneous process through which macroscopic structures are formed from basic microscopic constituents (e.g., molecules or colloids). By contrast, the formation of large biological molecules inside the cell (such as proteins or nucleic acids) is a process more akin to self-organization than to self-assembly, as it requires a constant supply of external energy. Recent studies have tried to merge self-assembly with self-organization by analyzing the assembly of self-propelled (or active) colloid-like particles whose motion is driven by a permanent source of energy. Here we present evidence that points to the fact that self-propulsion considerably enhances the assembly of polymers: self-propelled molecules are found to assemble faster into polymer-like structures than non self-propelled ones. The average polymer length increases towards a maximum as the self-propulsion force increases. Beyond this maximum, the average polymer length decreases due to the competition between bonding energy and disruptive forces that result from collisions. The assembly of active molecules might have promoted the formation of large pre-biotic polymers that could be the precursors of the informational polymers we observe nowadays.

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41

Bell, Dylan, Samuel Durrance, Daniel Kirk, Hector Gutierrez, Daniel Woodard, Jose Avendano, Joseph Sargent, et al. "Self-Assembly of Protein Fibrils in Microgravity." Gravitational and Space Research 6, no. 1 (July 20, 2020): 10–26. http://dx.doi.org/10.2478/gsr-2018-0002.

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AbstractDeposits of insoluble protein fibrils in human tissue are associated with amyloidosis and neurodegenerative diseases. Different proteins are involved in each disease; all are soluble in their native conformation in vivo, but by molecular self-assembly, they all form insoluble protein fibril deposits with a similar cross β-sheet structure. This paper reports the results of an experiment in molecular self-assembly carried out in microgravity on the International Space Station (ISS). The Self-Assembly in Biology and the Origin of Life (SABOL) experiment was designed to study the growth of lysozyme fibrils in microgravity. Lysozyme is a model protein that has been shown to replicate the aggregation processes of other amyloid proteins. Here the design and performance of the experimental hardware is described in detail. The flight experiment was carried to the ISS in the Dragon capsule of the SpaceX CRS-5 mission and returned to Earth after 32 days. The lysozyme fibrils formed in microgravity aboard the ISS show a distinctly different morphology compared to fibrils formed in the ground-control (G-C) experiment. The fibrils formed in microgravity are shorter, straighter, and thicker than those formed in the laboratory G-C experiment. For two incubation periods, (2) about 8.5 days and (3) about 14.5 days, the average ISS and G-C fibril diameters are respectively: \matrix{{Period\,2} \hfill & {} \hfill & {{D_{ISS}} = 7.5{\rm{nm}} \pm 31\% ,} \hfill \cr {} \hfill & {\rm and} \hfill & {{D_{G - C}} = 3.4{\rm{nm}} \pm 31\%} \hfill \cr {Period\,3} \hfill & {} \hfill & {{D_{ISS}} = 6.2{\rm{nm}} \pm 33\% ,} \hfill \cr {} \hfill & {\rm and} \hfill & {{D_{G - C}} = 3.6{\rm{nm}} \pm 33\% .}}

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42

Minamihata, K., K. Tsukamoto, M. Adachi, R. Shimizu, M. Mishina, R. Kuroki, and T. Nagamune. "Genetically fused charged peptides induce rapid crystallization of proteins." Chemical Communications 56, no. 27 (2020): 3891–94. http://dx.doi.org/10.1039/c9cc09529b.

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43

Kahraman, Osman, and Christoph A. Haselwandter. "Supramolecular organization of membrane proteins with anisotropic hydrophobic thickness." Soft Matter 15, no. 21 (2019): 4301–10. http://dx.doi.org/10.1039/c9sm00358d.

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Arancibia, Duxan, Matias Lira, Yocelin Cruz, Daniela P. Barrera, Carolina Montenegro-Venegas, Juan A. Godoy, Craig C. Garner, et al. "Serine–Arginine Protein Kinase SRPK2 Modulates the Assembly of the Active Zone Scaffolding Protein CAST1/ERC2." Cells 8, no. 11 (October 29, 2019): 1333. http://dx.doi.org/10.3390/cells8111333.

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Neurons release neurotransmitters at a specialized region of the presynaptic membrane, the active zone (AZ), where a complex meshwork of proteins organizes the release apparatus. The formation of this proteinaceous cytomatrix at the AZ (CAZ) depends on precise homo- and hetero-oligomerizations of distinct CAZ proteins. The CAZ protein CAST1/ERC2 contains four coiled-coil (CC) domains that interact with other CAZ proteins, but also promote self-assembly, which is an essential step for its integration during AZ formation. The self-assembly and synaptic recruitment of the Drosophila protein Bruchpilot (BRP), a partial homolog of CAST1/ERC2, is modulated by the serine-arginine protein kinase (SRPK79D). Here, we demonstrate that overexpression of the vertebrate SRPK2 regulates the self-assembly of CAST1/ERC2 in HEK293T, SH-SY5Y and HT-22 cells and the CC1 and CC4 domains are involved in this process. Moreover, the isoform SRPK2 forms a complex with CAST1/ERC2 when co-expressed in HEK293T and SH-SY5Y cells. More importantly, SRPK2 is present in brain synaptic fractions and synapses, suggesting that this protein kinase might control the level of self-aggregation of CAST1/ERC2 in synapses, and thereby modulate presynaptic assembly.

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Stel, Bart, Fernando Cometto, Behzad Rad, James J. De Yoreo, and Magalí Lingenfelder. "Dynamically resolved self-assembly of S-layer proteins on solid surfaces." Chemical Communications 54, no. 73 (2018): 10264–67. http://dx.doi.org/10.1039/c8cc04597f.

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Amărioarei, Alexandru, Frankie Spencer, Gefry Barad, Ana-Maria Gheorghe, Corina Iţcuş, Iris Tuşa, Ana-Maria Prelipcean, et al. "DNA-Guided Assembly for Fibril Proteins." Mathematics 9, no. 4 (February 19, 2021): 404. http://dx.doi.org/10.3390/math9040404.

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Current advances in computational modelling and simulation have led to the inclusion of computer scientists as partners in the process of engineering of new nanomaterials and nanodevices. This trend is now, more than ever, visible in the field of deoxyribonucleic acid (DNA)-based nanotechnology, as DNA’s intrinsic principle of self-assembly has been proven to be highly algorithmic and programmable. As a raw material, DNA is a rather unremarkable fabric. However, as a way to achieve patterns, dynamic behavior, or nano-shape reconstruction, DNA has been proven to be one of the most functional nanomaterials. It would thus be of great potential to pair up DNA’s highly functional assembly characteristics with the mechanic properties of other well-known bio-nanomaterials, such as graphene, cellulos, or fibroin. In the current study, we perform projections regarding the structural properties of a fibril mesh (or filter) for which assembly would be guided by the controlled aggregation of DNA scaffold subunits. The formation of such a 2D fibril mesh structure is ensured by the mechanistic assembly properties borrowed from the DNA assembly apparatus. For generating inexpensive pre-experimental assessments regarding the efficiency of various assembly strategies, we introduced in this study a computational model for the simulation of fibril mesh assembly dynamical systems. Our approach was based on providing solutions towards two main circumstances. First, we created a functional computational model that is restrictive enough to be able to numerically simulate the controlled aggregation of up to 1000s of elementary fibril elements yet rich enough to provide actionable insides on the structural characteristics for the generated assembly. Second, we used the provided numerical model in order to generate projections regarding effective ways of manipulating one of the the key structural properties of such generated filters, namely the average size of the openings (gaps) within these meshes, also known as the filter’s aperture. This work is a continuation of Amarioarei et al., 2018, where a preliminary version of this research was discussed.

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Khanikar, Rakesh Ruchel, Parismita Kalita, Monika Narzary, Deepjyoti Basumatary, Ashim Jyoti Bharati, Anurag Priyadarshi, R. Swaminathan, Heremba Bailung, and Kamatchi Sankaranarayanan. "Cold atmospheric plasma driven self-assembly in serum proteins: insights into the protein aggregation to biomaterials." RSC Advances 12, no. 40 (2022): 26211–19. http://dx.doi.org/10.1039/d2ra04318a.

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Rizzo, Daniel, Ross Beighley, James D. White, and Cristian Staii. "Controlling neuronal growth and connectivity via directed self-assembly of proteins." MRS Proceedings 1498 (2013): 207–12. http://dx.doi.org/10.1557/opl.2013.338.

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ABSTRACTMaterials that offer the ability to influence tissue regeneration are of vital importance to the field of Tissue Engineering. Because valid 3-dimensional scaffolds for nerve tissue are still in development, advances with 2-dimensional surfaces in vitro are necessary to provide a complete understanding of controlling regeneration. Here we present a method for controlling nerve cell growth on Au electrodes using Atomic Force Microscopy -aided protein assembly. After coating a gold surface in a self-assembling monolayer of alkanethiols, the Atomic Force Microscope tip can be used to remove regions of the self-assembling monolayer in order to produce well-defined patterns. If this process is then followed by submersion of the sample into a solution containing neuro-compatible proteins, they will self assemble on these exposed regions of gold, creating well-specified regions for promoted neuron growth.

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Subramani, Karthikeyan, Ameen Khraisat, and Anne George. "Self-Assembly of Proteins and Peptides and their Applications in Bionanotechnology." Current Nanoscience 4, no. 2 (May 1, 2008): 201–7. http://dx.doi.org/10.2174/157341308784340831.

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Hernandez-Garcia, Armando, Daniela J. Kraft, Anne F. J. Janssen, Paul H. H. Bomans, Nico A. J. M. Sommerdijk, Dominique M. E. Thies-Weesie, Marco E. Favretto, et al. "Design and self-assembly of simple coat proteins for artificial viruses." Nature Nanotechnology 9, no. 9 (August 24, 2014): 698–702. http://dx.doi.org/10.1038/nnano.2014.169.

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