Selective nucleophilic additions to poly(methacrylate)s containing isothiocyanate moieties in the side chains and their application in cross-linking

2014 ◽  
Vol 52 (13) ◽  
pp. 1832-1842 ◽  
Author(s):  
Ryota Seto ◽  
Kozo Matsumoto ◽  
Takeshi Endo
Keyword(s):  
Cross Linking ◽  
Nucleophilic Additions ◽  
Side Chains

scholarly journals Enzymatic Cross-Linking of Side Chains Generates a Modified Peptide with Four Hairpin-like Bicyclic Repeats

Biochemistry ◽  
2017 ◽  
Vol 56 (37) ◽  
pp. 4927-4930 ◽  
Author(s):  
Hyunbin Lee ◽  
Youngseon Park ◽  
Seokhee Kim
Keyword(s):  
Cross Linking ◽  
Side Chains

scholarly journals Influence of Cross-Linker Polarity on Selectivity towards Lysine Side Chains

2020 ◽  
Author(s):  
Jan Fiala ◽  
Zdeněk Kukačka ◽  
Petr Novák
Keyword(s):  
Structural Information ◽  
Protein Complexes ◽  
Water Soluble ◽  
Cross Linking ◽  
Side Chains ◽  
Model Protein ◽  
Cross Linker ◽  
Progressive Technology ◽  
The Impact ◽  
Chemical Cross Linking

The combination of chemical cross-linking and mass spectrometry is currently a progressive technology for deriving structural information of proteins and protein complexes. In addition, chemical cross-linking is a powerful tool for stabilizing macromolecular complexes for single particle cryo-electron microscopy. Broad pallets of cross-linking chemistry, currently available for the majority of cross-linking experiments, still rely on the amine-reactive N-hydroxysuccinimide esters targeting mainly N-termini and lysine side chains. These cross-linkers are divided into two groups: water soluble and water insoluble; and research teams prefer one or another speculating on the benefits of their choice. However, the effect of cross-linker polarity on the outcome of cross-linking reaction has never been studied. Herein, we use both polar (bis(sulfosuccinimidyl) glutarate) and non-polar (disuccinimidyl glutarate) cross-linkers and systematically investigated the impact of cross-linker hydrophobicity on resulting distance constraints, using bovine serum albumin as a model protein.

Photoinduced Bending Behaviour of Cross-linked Liquid Crystalline Polymers with High Cross-linking Densities

2014 ◽  
Vol 67 (4) ◽  
pp. 570 ◽  
Author(s):  
Zhen Jiang ◽  
Jiu-an Lv ◽  
Futao Chen ◽  
Jia Wei ◽  
Yanlei Yu
Keyword(s):  
Liquid Crystalline Polymer ◽  
Liquid Crystalline ◽  
Crystalline Polymer ◽  
Reverse Direction ◽  
Cross Linking ◽  
Side Chains ◽  
Material System ◽  
Crystalline Polymers ◽  
The Cross ◽  
Bending Behaviour

Highly cross-linked liquid crystalline polymer (CLCP) films with a long spacer and azobenzene chromophores (of varying concentrations and positioned differently) were prepared. The effects of various factors on the photoinduced bending behaviour of the highly CLCPs were explored. Long spacer groups and high cross-linking density resulted in considerably faster bending of the CLCP films relative to those reported in the literature that feature shorter spacer groups and smaller cross-linking densities. The azobenzene chromophores at the cross-linking points significantly influenced the photoinduced bending behaviour of the CLCP films relative to those at side chains. Furthermore, reduced concentrations of the azobenzene chromophores produced faster bending and larger photoinduced stress of the CLCP films that contained chromophores at the side chains as opposed to those incorporating chromophores at the cross-linking points. Moreover, the CLCP film with relatively low azobenzene concentration and small thickness exhibited bending in the reverse direction following maximum bending under continuous UV irradiation, thereby showing that photomobile behaviour of the material system.

scholarly journals Lysine and Arginine Side Chains in Glycosaminoglycan−Protein Complexes Investigated by NMR, Cross-Linking, and Mass Spectrometry: A Case Study of the Factor H−Heparin Interaction

2010 ◽  
Vol 132 (18) ◽  
pp. 6374-6381 ◽  
Author(s):  
Bärbel S. Blaum ◽  
Jon A. Deakin ◽  
Conny M. Johansson ◽  
Andrew P. Herbert ◽  
Paul N. Barlow ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Complexes ◽  
Factor H ◽  
Cross Linking ◽  
Side Chains ◽  
Heparin Interaction

Electrochromic pattern formation by photo cross-linking reaction of PEDOT side chains

2009 ◽  
Vol 17 (10) ◽  
pp. 791-796 ◽  
Author(s):  
Jeonghun Kim ◽  
Yuna Kim ◽  
Eunkyoung Kim
Keyword(s):  
Pattern Formation ◽  
Cross Linking ◽  
Side Chains

A cycloaddition approach to tricyclic taxoid skeletons

1995 ◽  
Vol 73 (12) ◽  
pp. 2239-2252 ◽  
Author(s):  
Yee-Fung Lu ◽  
Alex G. Fallis
Keyword(s):  
Diels Alder ◽  
Allylic Oxidation ◽  
Nucleophilic Additions ◽  
Side Chains ◽  
Diterpene Alkaloid ◽  
Thermal Cyclization ◽  
Protecting Group ◽  
Aromatic System ◽  
Microwave Assisted ◽  
Tricyclic Ketone

A cycloaddition approach to the functionalized tricyclo[9.3.1.03,8]pentadecene skeleton contained in Taxol® is described. The cyclohexenone 13 was converted as illustrated to the nitrile-aldehyde 24 to which the diene and acetylenic side chains were attached by sequential nucleophilic additions. Removal of the trimethylsilyl protecting group and Dess–Martin oxidation afforded the triene 35. Microwave-assisted thermal cyclization stereoselectively generated the tricyclic ketone 36 whose structure was further established by conversion to the aromatic system 37 upon treatment with 2,3-dichloro-5,6-dicyano-1,4-benzoquinone (DDQ). An epoxidation sequence was developed to introduce the epimeric C13 alcohol 47 as required for this cycloaddition strategy. Alternatively, an allylic oxidation (CrO3, 3,5-dimethylpyrazole) afforded the C13 ketone 49. Keywords: Taxol®, Diels–Alder, synthesis, diterpene, alkaloid.

scholarly journals Mutational Analysis of a Conserved Glutamic Acid Required for Self-Catalyzed Cross-Linking of Bacteriophage HK97 Capsids

2008 ◽  
Vol 83 (5) ◽  
pp. 2088-2098 ◽  
Author(s):  
Lindsay E. Dierkes ◽  
Craig L. Peebles ◽  
Brian A. Firek ◽  
Roger W. Hendrix ◽  
Robert L. Duda
Keyword(s):  
Glutamic Acid ◽  
Large Scale ◽  
Mutational Analysis ◽  
Chemical Mechanism ◽  
Proton Acceptor ◽  
Cross Linking ◽  
Side Chains ◽  
Cross Link ◽  
Cross Links ◽  
The Cross

ABSTRACT The capsid of bacteriophage HK97 is stabilized by ∼400 covalent cross-links between subunits which form without any action by external enzymes or cofactors. Cross-linking only occurs in fully assembled particles after large-scale structural changes bring together side chains from three subunits at each cross-linking site. Isopeptide cross-links form between asparagine and lysine side chains on two subunits. The carboxylate of glutamic acid 363 (E363) from a third subunit is found ∼2.4 Å from the isopeptide bond in the partly hydrophobic pocket that contains the cross-link. It was previously reported without supporting data that changing E363 to alanine abolishes cross-linking, suggesting that E363 plays a role in cross-linking. This alanine mutant and six additional substitutions for E363 were fully characterized and the proheads produced by the mutants were tested for their ability to cross-link under a variety of conditions. Aspartic acid and histidine substitutions supported cross-linking to a significant extent, while alanine, asparagine, glutamine, and tyrosine did not, suggesting that residue 363 acts as a proton acceptor during cross-linking. These results support a chemical mechanism, not yet fully tested, that incorporates this suggestion, as well as features of the structure at the cross-link site. The chemically identical isopeptide bonds recently documented in bacterial pili have a strikingly similar chemical geometry at their cross-linking sites, suggesting a common chemical mechanism with the phage protein, but the completely different structures and folds of the two proteins argues that the phage capsid and bacterial pilus proteins have achieved shared cross-linking chemistry by convergent evolution.

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