Self-Assembly of Alkali Lignin in Tetrahydrofuran

2012 ◽  
Vol 550-553 ◽  
pp. 57-61
Author(s):  
Hao Li ◽  
Yong Hong Deng ◽  
Kai Huang

Alkali lignin (AL) was used as a polyanion to form layer-by-layer self-assembled film with PDAC as a polycation. The effects of temperature and concentration on the adsorption characteristics of AL were investigated. Iodine was added into AL solutions to study the role of π-π interaction in self-assembly of AL and PDAC. Results show that the self-assembly of AL/PDAC is mainly driven by π-π interaction and electrostatic interaction. A higher temperature or a larger concentration can enhance the aggregation of lignin. I2 can form lignin–iodine charge–transfer complexes with AL to reduce the degree of aggregation of AL, so the adsorbed amount of AL decreases significantly with increasing iodine contents.

2019 ◽  
Vol 55 (17) ◽  
pp. 2481-2484 ◽  
Author(s):  
Wouter T. M. Van Gompel ◽  
Roald Herckens ◽  
Kristof Van Hecke ◽  
Bart Ruttens ◽  
Jan D'Haen ◽  
...  

This study broadens the family of 2D layered perovskites by the self-assembly of organic charge-transfer complexes in their organic layer.


2020 ◽  
Vol 27 (9) ◽  
pp. 923-929
Author(s):  
Gaurav Pandey ◽  
Prem Prakash Das ◽  
Vibin Ramakrishnan

Background: RADA-4 (Ac-RADARADARADARADA-NH2) is the most extensively studied and marketed self-assembling peptide, forming hydrogel, used to create defined threedimensional microenvironments for cell culture applications. Objectives: In this work, we use various biophysical techniques to investigate the length dependency of RADA aggregation and assembly. Methods: We synthesized a series of RADA-N peptides, N ranging from 1 to 4, resulting in four peptides having 4, 8, 12, and 16 amino acids in their sequence. Through a combination of various biophysical methods including thioflavin T fluorescence assay, static right angle light scattering assay, Dynamic Light Scattering (DLS), electron microscopy, CD, and IR spectroscopy, we have examined the role of chain-length on the self-assembly of RADA peptide. Results: Our observations show that the aggregation of ionic, charge-complementary RADA motifcontaining peptides is length-dependent, with N less than 3 are not forming spontaneous selfassemblies. Conclusion: The six biophysical experiments discussed in this paper validate the significance of chain-length on the epitaxial growth of RADA peptide self-assembly.


2021 ◽  
Author(s):  
Beatriz Matarranz ◽  
Goutam Ghosh ◽  
Ramesh Kandanelli ◽  
Angel Sampedro ◽  
Kalathil K. Kartha ◽  
...  

We unravel the relationship between conjugation length and self-assembly behaviour of oligophenyleneethynylenes (OPEs).


2007 ◽  
Vol 111 (51) ◽  
pp. 14233-14238 ◽  
Author(s):  
Guillaume Tresset ◽  
Wun Chet Davy Cheong ◽  
Yeng Ming Lam
Keyword(s):  
The Self ◽  

2017 ◽  
Vol 129 (43) ◽  
pp. 13473-13477 ◽  
Author(s):  
Shibaji Basak ◽  
Ishwar Singh ◽  
Annaleizle Ferranco ◽  
Jebreil Syed ◽  
Heinz-Bernhard Kraatz
Keyword(s):  

RSC Advances ◽  
2015 ◽  
Vol 5 (115) ◽  
pp. 95007-95013 ◽  
Author(s):  
A. Scelsi ◽  
B. Bochicchio ◽  
A. Smith ◽  
A. Saiani ◽  
A. Pepe

The self-assembly of an elastin-inspired triblock peptide into nanospheres highlights the important role of conformational flexibility and π–π stacking.


mBio ◽  
2018 ◽  
Vol 9 (5) ◽  
Author(s):  
Xiaoyu Sun ◽  
Serban L. Ilca ◽  
Juha T. Huiskonen ◽  
Minna M. Poranen

ABSTRACTDouble-stranded RNA (dsRNA) viruses package several RNA-dependent RNA polymerases (RdRp) together with their dsRNA genome into an icosahedral protein capsid known as the polymerase complex. This structure is highly conserved among dsRNA viruses but is not found in any other virus group. RdRp subunits typically interact directly with the main capsid proteins, close to the 5-fold symmetric axes, and perform viral genome replication and transcription within the icosahedral protein shell. In this study, we utilizedPseudomonasphage Φ6, a well-established virus self-assembly model, to probe the potential roles of the RdRp in dsRNA virus assembly. We demonstrated that Φ6 RdRp accelerates the polymerase complex self-assembly process and contributes to its conformational stability and integrity. We highlight the role of specific amino acid residues on the surface of the RdRp in its incorporation during the self-assembly reaction. Substitutions of these residues reduce RdRp incorporation into the polymerase complex during the self-assembly reaction. Furthermore, we determined that the overall transcription efficiency of the Φ6 polymerase complex increased when the number of RdRp subunits exceeded the number of genome segments. These results suggest a mechanism for RdRp recruitment in the polymerase complex and highlight its novel role in virion assembly, in addition to the canonical RNA transcription and replication functions.IMPORTANCEDouble-stranded RNA viruses infect a wide spectrum of hosts, including animals, plants, fungi, and bacteria. Yet genome replication mechanisms of these viruses are conserved. During the infection cycle, a proteinaceous capsid, the polymerase complex, is formed. An essential component of this capsid is the viral RNA polymerase that replicates and transcribes the enclosed viral genome. The polymerase complex structure is well characterized for many double-stranded RNA viruses. However, much less is known about the hierarchical molecular interactions that take place in building up such complexes. Using the bacteriophage Φ6 self-assembly system, we obtained novel insights into the processes that mediate polymerase subunit incorporation into the polymerase complex for generation of functional structures. The results presented pave the way for the exploitation and engineering of viral self-assembly processes for biomedical and synthetic biology applications. An understanding of viral assembly processes at the molecular level may also facilitate the development of antivirals that target viral capsid assembly.


Author(s):  
Fredrik C. Wieland ◽  
Mireille M.J.P.E. Sthijns ◽  
Thomas Geuens ◽  
Clemens A. van Blitterswijk ◽  
Vanessa L.S. LaPointe
Keyword(s):  
The Self ◽  

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