scholarly journals What Is the Assembly Pathway of a Conjugated Polymer From Solution to Thin Films?

2020 ◽  
Vol 8 ◽  
Author(s):  
Zhuang Xu ◽  
Kyung Sun Park ◽  
Ying Diao
Keyword(s):  
Conjugated Polymers ◽  
Critical Role ◽  
Domain Size ◽  
Hierarchical Assembly ◽  
Solution State ◽  
Assembly Pathway ◽  
Assembly Pathways ◽  
Hierarchical Morphology ◽  
Structural Characterizations ◽  
Polymer Assembly

The hierarchical assembly of conjugated polymers has gained much attention due to its critical role in determining optical/electrical/mechanical properties. The hierarchical morphology encompasses molecular-scale intramolecular conformation (torsion angle, chain folds) and intermolecular ordering (π–π stacking), mesoscale domain size, orientation and connectivity, and macroscale alignment and (para)crystallinity. Such complex morphology in the solid state is fully determined by the polymer assembly pathway in the solution state, which, in turn, is sensitively modulated by molecular structure and processing conditions. However, molecular pictures of polymer assembly pathways remain elusive due to the lack of detailed structural characterizations in the solution state and the lack of understanding on how various factors impact the assembly pathways. In this mini-review, we present possible assembly pathways of conjugated polymers and their characteristics across length scales. Recent advances in understanding and controlling of assembly pathways are highlighted. We also discuss the current gap in our knowledge of assembly pathways, with future perspectives on research needed on this topic.

Conductive Polymers Based on Phenothiazine-Benzothiadiazole: Synthesis, Characterization of Photovoltaics

2013 ◽  
Vol 634-638 ◽  
pp. 2643-2650 ◽  
Author(s):  
Dae Hee Yun ◽  
Han Sol Yoo ◽  
Tae Won Ko ◽  
Yong Sung Park ◽  
Je Wan Woo
Keyword(s):  
Conjugated Polymers ◽  
Power Conversion ◽  
Coupling Reaction ◽  
Band Gap Energy ◽  
Suzuki Coupling Reaction ◽  
Gap Energy ◽  
Solution State ◽  
Conversion Efficiencies ◽  
Film State

Two new π-conjugated polymers (Poly[(N-10’-(octan-3-yl)-phenothiazin-3,7-ylene)-alt- (4’,7’-bis(thiophen-2-yl)benzo[c][1,2,5]thiadiazole)] (PoPTZ-BT-BTD), Poly[(N-10`-(octan-3-yl) -phenothiazin-3,7-ylene)-alt-(4’,7’-bis(thiophen-2-yl)-5,6-bis(octyloxy)benzo[c][1,2,5]thiadiazole)] (PoPTZ-BT-BoBTD) ) were synthesized through the Suzuki coupling reaction for organic photovoltaics (OPVs), and their optical and electrochemical properties were analyzed. Their wavelength of maximun absorption was 526 nm and 506 nm in solution state, repectively, and 560 nm and 522 nm in film state, respectively. Their band-gap energy was 2.01 eV and 2.09 eV in solution state, and 1.82 eV and 1.91 eV in film state, respectively. The results of analysis of the chrateristics of photovoltaics, 0.79 % and 0.99 % of the maximum power conversion efficiencies (PCE), repectively.

Ordered Solid‐State Microstructures of Conjugated Polymers Arising from Solution‐State Aggregation

2020 ◽  
Vol 132 (40) ◽  
pp. 17620-17624
Author(s):  
Ze‐Fan Yao ◽  
Zi‐Yuan Wang ◽  
Hao‐Tian Wu ◽  
Yang Lu ◽  
Qi‐Yi Li ◽  
...  
Keyword(s):  
Solid State ◽  
Conjugated Polymers ◽  
Solution State ◽  
State Aggregation

scholarly journals Hierarchical Assembly Pathways of Spermine Induced Tubulin Conical-Spiral Architectures

2020 ◽  
Author(s):  
Raviv Dharan ◽  
Asaf Shemesh ◽  
Abigail Millgram ◽  
Yael Levi-Kalisman ◽  
Israel Ringel ◽  
...  
Keyword(s):  
Progressive Increase ◽  
Hexagonal Symmetry ◽  
Time Resolved ◽  
Hierarchical Assembly ◽  
X Ray Scattering ◽  
Cellular Factors ◽  
Hierarchical Architectures ◽  
Assembly Pathways ◽  
Insight Into

<p>Tubulin, an essential cytoskeletal protein, assembles into various morphologies by interacting with cellular factors. Spermine, an endogenous polyamine, promotes and stabilizes tubulin assemblies. Yet, the assembled structures and their formation pathways are poorly known. Here we show that spermine induced tubulin to assemble <i>in vitro</i> into hierarchical architectures, based on a tubulin conical-spiral (TCS) subunit. Using solution X-ray scattering and cryo-TEM, we showed that with progressive increase of spermine concentration, tubulin-dimers assembled into a tubulin helical-pitch (or a short TCS), TCSs, TCS that stacked into tubes through base-to-top packing, antiparallel bundles of TCS tubes in a quasi-hexagonal symmetry, and eventually twisted hexagonal bundles of inverted tubulin tubules. Time-resolved experiments revealed that tubulin assemblies formed at low spermine concentrations were precursors of the assemblies formed at higher spermine concentrations. The results provide insight into the variety of morphologies that tubulin can form, and contribute to our understanding of the fundamental interactions that control the composition and construction of protein-based biomaterials.</p>

Ordered Solid‐State Microstructures of Conjugated Polymers Arising from Solution‐State Aggregation

2020 ◽  
Vol 59 (40) ◽  
pp. 17467-17471 ◽  
Author(s):  
Ze‐Fan Yao ◽  
Zi‐Yuan Wang ◽  
Hao‐Tian Wu ◽  
Yang Lu ◽  
Qi‐Yi Li ◽  
...  
Keyword(s):  
Solid State ◽  
Conjugated Polymers ◽  
Solution State ◽  
State Aggregation

scholarly journals Asymmetrizing an icosahedral virus capsid by hierarchical assembly of subunits with designed asymmetry

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Zhongchao Zhao ◽  
Joseph Che-Yen Wang ◽  
Mi Zhang ◽  
Nicholas A. Lyktey ◽  
Martin F. Jarrold ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Medical Applications ◽  
Virus Capsid ◽  
Viral Capsids ◽  
Hierarchical Assembly ◽  
Assembly Pathway ◽  
B Virus ◽  
Icosahedral Virus ◽  
Surface Chemistries ◽  
Virus Capsid Protein

AbstractSymmetrical protein complexes are ubiquitous in biology. Many have been re-engineered for chemical and medical applications. Viral capsids and their assembly are frequent platforms for these investigations. A means to create asymmetric capsids may expand applications. Here, starting with homodimeric Hepatitis B Virus capsid protein, we develop a heterodimer, design a hierarchical assembly pathway, and produce asymmetric capsids. In the heterodimer, the two halves have different growth potentials and assemble into hexamers. These preformed hexamers can nucleate co-assembly with other dimers, leading to Janus-like capsids with a small discrete hexamer patch. We can remove the patch specifically and observe asymmetric holey capsids by cryo-EM reconstruction. The resulting hole in the surface can be refilled with fluorescently labeled dimers to regenerate an intact capsid. In this study, we show how an asymmetric subunit can be used to generate an asymmetric particle, creating the potential for a capsid with different surface chemistries.

Encoding hierarchical assembly pathways of proteins with DNA

2021 ◽  
Vol 118 (40) ◽  
pp. e2106808118
Author(s):  
Oliver G. Hayes ◽  
Benjamin E. Partridge ◽  
Chad A. Mirkin
Keyword(s):  
Dna Sequence ◽  
Building Blocks ◽  
Chemical Information ◽  
Dna Interactions ◽  
Sequence Design ◽  
Hierarchical Assembly ◽  
Direct Assembly ◽  
Dna Sequence Design ◽  
Dna Materials ◽  
Assembly Pathways

The structural and functional diversity of materials in nature depends on the controlled assembly of discrete building blocks into complex architectures via specific, multistep, hierarchical assembly pathways. Achieving similar complexity in synthetic materials through hierarchical assembly is challenging due to difficulties with defining multiple recognition areas on synthetic building blocks and controlling the sequence through which those recognition sites direct assembly. Here, we show that we can exploit the chemical anisotropy of proteins and the programmability of DNA ligands to deliberately control the hierarchical assembly of protein–DNA materials. Through DNA sequence design, we introduce orthogonal DNA interactions with disparate interaction strengths (“strong” and “weak”) onto specific geometric regions of a model protein, stable protein 1 (Sp1). We show that the spatial encoding of DNA ligands leads to highly directional assembly via strong interactions and that, by design, the first stage of assembly increases the multivalency of weak DNA–DNA interactions that give rise to an emergent second stage of assembly. Furthermore, we demonstrate that judicious DNA design not only directs assembly along a given pathway but can also direct distinct structural outcomes from a single pathway. This combination of protein surface and DNA sequence design allows us to encode the structural and chemical information necessary into building blocks to program their multistep hierarchical assembly. Our findings represent a strategy for controlling the hierarchical assembly of proteins to realize a diverse set of protein–DNA materials by design.

scholarly journals Hierarchical Assembly Pathways of Spermine-Induced Tubulin Conical-Spiral Architectures

ACS Nano ◽  
2021 ◽  
Author(s):  
Raviv Dharan ◽  
Asaf Shemesh ◽  
Abigail Millgram ◽  
Ran Zalk ◽  
Gabriel A. Frank ◽  
...  
Keyword(s):  
Hierarchical Assembly ◽  
Assembly Pathways

Distinct solid and solution state self-assembly pathways of RADA16-I designer peptide

2013 ◽  
Vol 19 (8) ◽  
pp. 477-484 ◽  
Author(s):  
Ashley R. Cormier ◽  
Juan M. Lopez-Majada ◽  
Rufina G. Alamo ◽  
Anant K. Paravastu
Keyword(s):  
Self Assembly ◽  
Solution State ◽  
Assembly Pathways

scholarly journals In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals

Biomolecules ◽  
2019 ◽  
Vol 9 (6) ◽  
pp. 213 ◽  
Author(s):  
Minghui Bai ◽  
Xian Zhao ◽  
Kazutaka Sahara ◽  
Yuki Ohte ◽  
Yuko Hirano ◽  
...  
Keyword(s):  
26S Proteasome ◽  
Core Particle ◽  
Proteasome Subunit ◽  
Ubiquitinated Proteins ◽  
Assembly Pathway ◽  
Assembly Mechanism ◽  
Depth Analysis ◽  
Regulatory Particle ◽  
Assembly Intermediate ◽  
Assembly Pathways

The 26S proteasome is a key player in the degradation of ubiquitinated proteins, comprising a 20S core particle (CP) and a 19S regulatory particle (RP). The RP is further divided into base and lid subcomplexes, which are assembled independently from each other. We have previously demonstrated the assembly pathway of the CP and the base by observing assembly intermediates resulting from knockdowns of each proteasome subunit and the assembly chaperones. In this study, we examine the assembly pathway of the mammalian lid, which remains to be elucidated. We show that the lid assembly pathway is conserved between humans and yeast. The final step is the incorporation of Rpn12 into the assembly intermediate consisting of two modular complexes, Rpn3-7-15 and Rpn5-6-8-9-11, in both humans and yeast. Furthermore, we dissect the assembly pathways of the two modular complexes by the knockdown of each lid subunit.

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