Pyridazine-3,6-diol-annulated Tetrathiafulvalene: Self-assembly and Fiber Formation Triggered by Diamine Addition

2015 ◽  
Vol 44 (4) ◽  
pp. 448-450 ◽  
Author(s):  
Ryota Inoue ◽  
Masashi Hasegawa ◽  
Yasuhiro Mazaki
2013 ◽  
Vol 52 (32) ◽  
pp. 8266-8270 ◽  
Author(s):  
Mark P. Del Borgo ◽  
Adam I. Mechler ◽  
Daouda Traore ◽  
Craig Forsyth ◽  
Jacqueline A. Wilce ◽  
...  

MRS Advances ◽  
2016 ◽  
Vol 1 (11) ◽  
pp. 711-716 ◽  
Author(s):  
Robabeh Gharaei ◽  
Giuseppe Tronci ◽  
Robert P. Davies ◽  
Parikshit Goswami ◽  
Stephen J. Russell

ABSTRACTSelf-assembling peptides (SAPs) have the ability to spontaneously assemble into ordered nanostructures enabling the manufacture of ‘designer’ nanomaterials. The reversible molecular association of SAPs has been shown to offer great promise in therapeutics via for example, the design of biomimetic assemblies for hard tissue regeneration. This could be further exploited for novel nano/micro diagnostic tools. However, self-assembled peptide gels are often associated with inherent weak and transient mechanical properties. Their incorporation into polymeric matrices has been considered as a potential strategy to enhance their mechanical stability. This study focuses on the incorporation of an 11-residue peptide, P11-8 (peptide sequence: CH3CO-Gln-Gln-Arg-Phe-Orn-Trp-Orn-Phe-Glu-Gln-Gln-NH2) within a fibrous scaffold of poly (ε-caprolactone) (PCL). In this study an electrospinning technique was used to fabricate a biomimetic porous scaffold out of a solution of P11-8 and PCL which resulted in a biphasic structure composed of submicron fibers (diameter of 100-700 nm) and nanofibers (diameter of 10-100 nm). The internal morphology of the fabric and its micro-structure can be easily controlled by changing the peptide concentration. The secondary conformation of P11-8 was investigated in the as-spun fibers by ATR-FTIR spectroscopy and it is shown that peptide self-assembly into β-sheet tapes has taken place during fiber formation and the deposition of the fibrous web.


Soft Matter ◽  
2013 ◽  
Vol 9 (38) ◽  
pp. 9111 ◽  
Author(s):  
Jérôme J. Crassous ◽  
Pierre-Eric Millard ◽  
Adriana M. Mihut ◽  
Alexander Wittemann ◽  
Markus Drechsler ◽  
...  

Author(s):  
Michael R. Lewis ◽  
Robert Josephs

Sickle cell disease is caused by the self assembly of deoxy-sickle hemoglobin (HbS) into fibers which rigidify and distort red cells. Fiber assembly is auto-catalytic in that the surface of existing fibers acts as a nucleating template for the assembly of new fibers (heterogeneous nucleation). Thus fibers are found typically as bundles of aligned particles. Understanding fiber-fiber interaction is crucial to understanding the pathology of fiber formation. Moreover, disrupting fiber-fiber interactions would likely ameliorate the severity of the disease. We have obtained images of both laterally associated and isolated fibers by cryo-electron microscopy (Figure 1). Optical diffraction indicates that laterally associated fibers tend to have much better long range order than isolated fibers. This observation suggests that deoxy-HbS fibers are more disordered when they are not mechanically coupled by inter-fiber contacts. In this study we assess the effects of fiber-fiber interactions on torsional disorder of deoxy-HbS fibers.


2020 ◽  
Author(s):  
Franziska Jehle ◽  
Tobias Priemel ◽  
Michael Strauss ◽  
Peter Fratzl ◽  
Luca Bertinetti ◽  
...  

Protein-based biological materials are important role models for the design and fabrication of next generation advanced polymers. Marine mussels (Mytilus spp.) fabricate hierarchically structured collagenous fibers known as byssal threads via bottom-up supramolecular assembly of fluid protein precursors. The high degree of structural organization in byssal threads is intimately linked to their exceptional toughness and self-healing capacity. Here, we investigated the hypothesis that multidomain collagen precursor proteins, known as preCols, are stored in secretory vesicles as a colloidal liquid crystal (LC) phase prior to thread self-assembly. Using advanced electron microscopy methods, including scanning TEM and FIB-SEM, we visualized the detailed smectic preCol LC nanostructure in 3D, including various LC defects, confirming this hypothesis and providing quantitative insights into the mesophase structure. In light of these findings, we performed an in-depth comparative analysis of preCol protein sequences from multiple Mytilid species revealing that the smectic organization arises from an evolutionarily conserved ABCBA penta-block co-polymer-like primary structure based on demarcations in hydropathy and charge distribution, as well as terminal pH-responsive domains<br>that trigger fiber formation. These distilled supramolecular assembly principles provide inspiration and strategies for sustainable assembly of nanostructured polymeric materials for<br>potential applications in engineering and biomedical applications.


2020 ◽  
Author(s):  
Franziska Jehle ◽  
Tobias Priemel ◽  
Michael Strauss ◽  
Peter Fratzl ◽  
Luca Bertinetti ◽  
...  

Protein-based biological materials are important role models for the design and fabrication of next generation advanced polymers. Marine mussels (Mytilus spp.) fabricate hierarchically structured collagenous fibers known as byssal threads via bottom-up supramolecular assembly of fluid protein precursors. The high degree of structural organization in byssal threads is intimately linked to their exceptional toughness and self-healing capacity. Here, we investigated the hypothesis that multidomain collagen precursor proteins, known as preCols, are stored in secretory vesicles as a colloidal liquid crystal (LC) phase prior to thread self-assembly. Using advanced electron microscopy methods, including scanning TEM and FIB-SEM, we visualized the detailed smectic preCol LC nanostructure in 3D, including various LC defects, confirming this hypothesis and providing quantitative insights into the mesophase structure. In light of these findings, we performed an in-depth comparative analysis of preCol protein sequences from multiple Mytilid species revealing that the smectic organization arises from an evolutionarily conserved ABCBA penta-block co-polymer-like primary structure based on demarcations in hydropathy and charge distribution, as well as terminal pH-responsive domains<br>that trigger fiber formation. These distilled supramolecular assembly principles provide inspiration and strategies for sustainable assembly of nanostructured polymeric materials for<br>potential applications in engineering and biomedical applications.


2021 ◽  
Vol 118 (38) ◽  
pp. e2100496118
Author(s):  
Tiantian Fan ◽  
Ruiqi Qin ◽  
Yan Zhang ◽  
Jingxia Wang ◽  
Jing-Song Fan ◽  
...  

Natural spider silk with extraordinary mechanical properties is typically spun from more than one type of spidroin. Although the main components of various spider silks have been widely studied, little is known about the molecular role of the minor silk components in spidroin self-assembly and fiber formation. Here, we show that the minor component of spider eggcase silk, TuSp2, not only accelerates self-assembly but remarkably promotes molecular chain alignment of spidroins upon physical shearing. NMR structure of the repetitive domain of TuSp2 reveals that its dimeric structure with unique charged surface serves as a platform to recruit different domains of the main eggcase component TuSp1. Artificial fiber spun from the complex between TuSp1 and TuSp2 minispidroins exhibits considerably higher strength and Young’s modulus than its native counterpart. These results create a framework for rationally designing silk biomaterials based on distinct roles of silk components.


1995 ◽  
Vol 414 ◽  
Author(s):  
G. D. Pins ◽  
D. L. Christiansen ◽  
R. Patel ◽  
F. H. Silver

AbstractThe primary goal of the biomaterials scientist and tissue engineer is to create a biocompatible implant which mimics the mechanical and morphological properties of the tissue being replaced. In vitro experimentation has documented the propensity of soluble type I collagen to self-assemble and form microscopic collagen fibrils with periodic banding analogous to native collagen fiber. Our laboratory has further investigated in vitro self-assembly by incorporating several of the “natural” processes into a multi-step fiber formation procedure which generates macroscopic collagen fiber from its molecular constituents. Results of uniaxial tensile tests and ultrastructural analyses indicate that these coextruded and stretched collagen fibers have mechanical properties and fibrillar substructure comparable to that observed in native collagen fiber.


2019 ◽  
Vol 59 (6) ◽  
pp. 1690-1699 ◽  
Author(s):  
Alexander Baer ◽  
Stephan Schmidt ◽  
Georg Mayer ◽  
Matthew J Harrington

Abstract Many organisms have evolved a capacity to form biopolymeric fibers outside their bodies for functions such as defense, prey capture, attachment, and protection. In particular, the adhesive capture slime of onychophorans (velvet worms) is remarkable for its ability to rapidly form stiff fibers through mechanical drawing. Notably, fibers that are formed ex vivo from extracted slime can be dissolved in water and new fibers can be drawn from the solution, indicating that fiber formation is encoded in the biomolecules that comprise the slime. This review highlights recent findings on the biochemical and physicochemical principles guiding this circular process in the Australian onychophoran Euperipatoides rowelli. A multiscale cross-disciplinary approach utilizing techniques from biology, biochemistry, physical chemistry, and materials science has revealed that the slime is a concentrated emulsion of nanodroplets comprised primarily of proteins, stabilized via electrostatic interactions, possibly in a coacervate phase. Upon mechanical agitation, droplets coalesce, leading to spontaneous self-assembly and fibrillation of proteins—a completely reversible process. Recent investigations highlight the importance of subtle transitions in protein structure and charge balance. These findings have clear relevance for better understanding this adaptive prey capture behavior and providing inspiration toward sustainable polymer processing.


2013 ◽  
Vol 125 (32) ◽  
pp. 8424-8428 ◽  
Author(s):  
Mark P. Del Borgo ◽  
Adam I. Mechler ◽  
Daouda Traore ◽  
Craig Forsyth ◽  
Jacqueline A. Wilce ◽  
...  

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