Hydrogen Bond Interactions Mediate Hierarchical Self-Assembly of POSS-Containing Block Copolymers Blended with Phenolic Resin

2014 ◽  
Vol 47 (24) ◽  
pp. 8709-8721 ◽  
Author(s):  
Chin-Wei Chiou ◽  
Yung-Chih Lin ◽  
Lei Wang ◽  
Rina Maeda ◽  
Teruaki Hayakawa ◽  
...  
2018 ◽  
Author(s):  
Sjors Bakels ◽  
E.M. Meijer ◽  
Mart Greuell ◽  
Sebastiaan Porskamp ◽  
George Rouwhorst ◽  
...  

Peptide aggregation, the self-assembly of peptides into structured beta-sheet fibril structures, is driven by a combination of intra- and intermolecular interactions. Here, the interplay between intramolecular and formed inter-sheet hydrogen bonds and the effect of dispersion interactions on the formation of neutral, isolated, peptide dimers is studied by infrared action spectroscopy. Therefore, four different homo- and hetereogeneous dimers formed from three different alanine-based model peptides have been studied under controlled and isolated conditions. The peptides differ from one another in the presence and location of a UV chromophore containing cap on either the C- or N-terminus. Conformations of the monomers of the peptides direct the final dimer structure: strongly hydrogen bonded or folded structures result in weakly bound dimers. Here the intramolecular hydrogen bonds are favored over new intermolecular hydrogen bond interactions. In contrast, linearly folded monomers are the ideal template to form parallel beta-sheet type structures. The weak intramolecular hydrogen bonds present in the linear monomers are replaced by the stronger inter-sheet hydrogen bond interactions. The influence of π-π disperion interactions on the structure of the dimer is minimal, the phenyl rings have the tendency to fold away from the peptide backbone to favour intermolecular hydrogen bond interactions. Quantum chemical calculations confirm our experimental observations.


2018 ◽  
Vol 39 (6) ◽  
pp. 1700783 ◽  
Author(s):  
Shuai Huang ◽  
Linlin Pang ◽  
Yuxuan Chen ◽  
Liming Zhou ◽  
Shaoming Fang ◽  
...  

1996 ◽  
pp. 899-900 ◽  
Author(s):  
Mubarik M. Chowdhry ◽  
D. Michael P. Mingos ◽  
Andrew J. P. White ◽  
David J. Williams

2018 ◽  
Author(s):  
Sjors Bakels ◽  
E.M. Meijer ◽  
Mart Greuell ◽  
Sebastiaan Porskamp ◽  
George Rouwhorst ◽  
...  

Peptide aggregation, the self-assembly of peptides into structured beta-sheet fibril structures, is driven by a combination of intra- and intermolecular interactions. Here, the interplay between intramolecular and formed inter-sheet hydrogen bonds and the effect of dispersion interactions on the formation of neutral, isolated, peptide dimers is studied by infrared action spectroscopy. Therefore, four different homo- and hetereogeneous dimers formed from three different alanine-based model peptides have been studied under controlled and isolated conditions. The peptides differ from one another in the presence and location of a UV chromophore containing cap on either the C- or N-terminus. Conformations of the monomers of the peptides direct the final dimer structure: strongly hydrogen bonded or folded structures result in weakly bound dimers. Here the intramolecular hydrogen bonds are favored over new intermolecular hydrogen bond interactions. In contrast, linearly folded monomers are the ideal template to form parallel beta-sheet type structures. The weak intramolecular hydrogen bonds present in the linear monomers are replaced by the stronger inter-sheet hydrogen bond interactions. The influence of π-π disperion interactions on the structure of the dimer is minimal, the phenyl rings have the tendency to fold away from the peptide backbone to favour intermolecular hydrogen bond interactions. Quantum chemical calculations confirm our experimental observations.


Soft Matter ◽  
2016 ◽  
Vol 12 (11) ◽  
pp. 2887-2893 ◽  
Author(s):  
Christianus M. A. Leenders ◽  
Matthew B. Baker ◽  
Imke A. B. Pijpers ◽  
René P. M. Lafleur ◽  
Lorenzo Albertazzi ◽  
...  

The self-assembly of a family of benzene-1,3,5-tricarboxamides (BTAs) in water is studied systematically to elucidate the role of hydrophobic and hydrogen-bond interactions.


2006 ◽  
Vol 937 ◽  
Author(s):  
Margarita Garcia ◽  
E.W. Meijer ◽  
Albertus Schenning

ABSTRACTA variety of α, α'-subtituted quaterthiophenes containing ester, amide and polymerizable side chains have been synthesized and fully characterized. The self-assembly properties of these oligothiophenes were studied as function of the side chain. Introduction of amide functionalities highly promotes the self-assembly via π-stacking and hydrogen bond interactions, while the lack of amides prevent aggregate formation. Initial experiments show that by introducing a sorbyl moiety as a polymerizable group it is possible to achieve covalent fixation of the oligothiophene units in the self-assembled state.


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