Protein-Mimetic Self-Assembly with Synthetic Macromolecules

2021 ◽  
Author(s):  
Meredith H. Barbee ◽  
Zoe M. Wright ◽  
Benjamin P. Allen ◽  
Hailey F. Taylor ◽  
Emily F. Patteson ◽  
...  
2020 ◽  
Author(s):  
Maria-Nefeli Antonopoulou ◽  
Richard Whitfield ◽  
Nghia Truong ◽  
Athina Anastasaki

<p>Controlling monomer sequence in synthetic macromolecules is a major challenge in polymer science and the order of building blocks has already been demonstrated to determine macromolecular folding, self-assembly and fundamental polymer properties. Dispersity is another key parameter in material design, with both low and high dispersity polymers displaying complementary properties and functions. However, synthetic approaches that can simultaneously control both sequence and dispersity remain experimentally unattainable. Here we report a simple, one pot, and rapid synthesis of sequence-controlled multiblocks with on demand control over dispersity while maintaining high livingness, excellent agreement between theoretical and experimental molecular weights and quantitative yields. Key to our approach is the regulation in chain transfer agent activity during controlled radical polymerization that enables the preparation of multiblocks with gradually ascending (<i>Ɖ</i>=1.16 →1.60), descending (<i>Ɖ</i>=1.66 →1.22), alternating low and high dispersity values (<i>Ɖ</i>=1.17 →1.61 →1.24 →1.70 →1.26) or any combination thereof. The enormous potential of our methodology was further demonstrated through the impressive synthesis of highly ordered pentablock, octablock and decablock copolymers yielding the first generation of multiblocks with concurrent control over both sequence and dispersity.</p>


2020 ◽  
Author(s):  
Maria-Nefeli Antonopoulou ◽  
Richard Whitfield ◽  
Nghia Truong ◽  
Athina Anastasaki

<p>Controlling monomer sequence in synthetic macromolecules is a major challenge in polymer science and the order of building blocks has already been demonstrated to determine macromolecular folding, self-assembly and fundamental polymer properties. Dispersity is another key parameter in material design, with both low and high dispersity polymers displaying complementary properties and functions. However, synthetic approaches that can simultaneously control both sequence and dispersity remain experimentally unattainable. Here we report a simple, one pot, and rapid synthesis of sequence-controlled multiblocks with on demand control over dispersity while maintaining high livingness, excellent agreement between theoretical and experimental molecular weights and quantitative yields. Key to our approach is the regulation in chain transfer agent activity during controlled radical polymerization that enables the preparation of multiblocks with gradually ascending (<i>Ɖ</i>=1.16 →1.60), descending (<i>Ɖ</i>=1.66 →1.22), alternating low and high dispersity values (<i>Ɖ</i>=1.17 →1.61 →1.24 →1.70 →1.26) or any combination thereof. The enormous potential of our methodology was further demonstrated through the impressive synthesis of highly ordered pentablock, octablock and decablock copolymers yielding the first generation of multiblocks with concurrent control over both sequence and dispersity.</p>


Science ◽  
2013 ◽  
Vol 341 (6146) ◽  
pp. 1238149 ◽  
Author(s):  
Jean-François Lutz ◽  
Makoto Ouchi ◽  
David R. Liu ◽  
Mitsuo Sawamoto

Sequence-controlled polymers are macromolecules in which monomer units of different chemical nature are arranged in an ordered fashion. The most prominent examples are biological and have been studied and used primarily by molecular biologists and biochemists. However, recent progress in protein- and DNA-based nanotechnologies has shown the relevance of sequence-controlled polymers to nonbiological applications, including data storage, nanoelectronics, and catalysis. In addition, synthetic polymer chemistry has provided interesting routes for preparing nonnatural sequence-controlled polymers. Although these synthetic macromolecules do not yet compare in functional scope with their natural counterparts, they open up opportunities for controlling the structure, self-assembly, and macroscopic properties of polymer materials.


2015 ◽  
Vol 6 (37) ◽  
pp. 6623-6631 ◽  
Author(s):  
Nese Cakir ◽  
Gurkan Hizal ◽  
C. Remzi Becer

Incorporating monomers into sequence-defined synthetic macromolecules endows them to mimic nature which results in key residues being anchored in the molecular recognition pattern.


Author(s):  
D. Reis ◽  
B. Vian ◽  
J. C. Roland

Wall morphogenesis in higher plants is a problem still open to controversy. Until now the possibility of a transmembrane control and the involvement of microtubules were mostly envisaged. Self-assembly processes have been observed in the case of walls of Chlamydomonas and bacteria. Spontaneous gelling interactions between xanthan and galactomannan from Ceratonia have been analyzed very recently. The present work provides indications that some processes of spontaneous aggregation could occur in higher plants during the formation and expansion of cell wall.Observations were performed on hypocotyl of mung bean (Phaseolus aureus) for which growth characteristics and wall composition have been previously defined.In situ, the walls of actively growing cells (primary walls) show an ordered three-dimensional organization (fig. 1). The wall is typically polylamellate with multifibrillar layers alternately transverse and longitudinal. Between these layers intermediate strata exist in which the orientation of microfibrils progressively rotates. Thus a progressive change in the morphogenetic activity occurs.


Author(s):  
M. Kessel ◽  
R. MacColl

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.


Author(s):  
Alan S. Rudolph ◽  
Ronald R. Price

We have employed cryoelectron microscopy to visualize events that occur during the freeze-drying of artificial membranes by employing real time video capture techniques. Artificial membranes or liposomes which are spherical structures within internal aqueous space are stabilized by water which provides the driving force for spontaneous self-assembly of these structures. Previous assays of damage to these structures which are induced by freeze drying reveal that the two principal deleterious events that occur are 1) fusion of liposomes and 2) leakage of contents trapped within the liposome [1]. In the past the only way to access these events was to examine the liposomes following the dehydration event. This technique allows the event to be monitored in real time as the liposomes destabilize and as water is sublimed at cryo temperatures in the vacuum of the microscope. The method by which liposomes are compromised by freeze-drying are largely unknown. This technique has shown that cryo-protectants such as glycerol and carbohydrates are able to maintain liposomal structure throughout the drying process.


Author(s):  
M. Sarikaya ◽  
J. T. Staley ◽  
I. A. Aksay

Biomimetics is an area of research in which the analysis of structures and functions of natural materials provide a source of inspiration for design and processing concepts for novel synthetic materials. Through biomimetics, it may be possible to establish structural control on a continuous length scale, resulting in superior structures able to withstand the requirements placed upon advanced materials. It is well recognized that biological systems efficiently produce complex and hierarchical structures on the molecular, micrometer, and macro scales with unique properties, and with greater structural control than is possible with synthetic materials. The dynamism of these systems allows the collection and transport of constituents; the nucleation, configuration, and growth of new structures by self-assembly; and the repair and replacement of old and damaged components. These materials include all-organic components such as spider webs and insect cuticles (Fig. 1); inorganic-organic composites, such as seashells (Fig. 2) and bones; all-ceramic composites, such as sea urchin teeth, spines, and other skeletal units (Fig. 3); and inorganic ultrafine magnetic and semiconducting particles produced by bacteria and algae, respectively (Fig. 4).


Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


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