scholarly journals Self-assembly and biological activities of ionic liquid crystals derived from aromatic amino acids

2018 ◽  
Vol 20 (31) ◽  
pp. 20371-20381 ◽  
Author(s):  
Manuel M. Neidhardt ◽  
Katharina Schmitt ◽  
Angelika Baro ◽  
Carmen Schneider ◽  
Ursula Bilitewski ◽  
...  

Does the mesomorphic behaviour of l-amino acid-based ILCs correlate with biological activity?

Soft Matter ◽  
2017 ◽  
Vol 13 (45) ◽  
pp. 8379-8391 ◽  
Author(s):  
Korinna Bader ◽  
Manuel M. Neidhardt ◽  
Tobias Wöhrle ◽  
Robert Forschner ◽  
Angelika Baro ◽  
...  

Introduction of charge simply converted non-conventional tyrosine/crown ether liquid crystals into ionic liquid crystals under change of mesophase type.


2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.


2020 ◽  
Vol 59 (26) ◽  
pp. 10557-10565
Author(s):  
Juri Litterscheidt ◽  
Jeffrey S. Bandar ◽  
Max Ebert ◽  
Robert Forschner ◽  
Korinna Bader ◽  
...  

2008 ◽  
Vol 37 (5) ◽  
pp. 538-539 ◽  
Author(s):  
Sanami Yazaki ◽  
Yuko Kamikawa ◽  
Masafumi Yoshio ◽  
Atsushi Hamasaki ◽  
Tomohiro Mukai ◽  
...  

2013 ◽  
Vol 19 (47) ◽  
pp. 16058-16065 ◽  
Author(s):  
Markus Mansueto ◽  
Wolfgang Frey ◽  
Sabine Laschat

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.


ChemInform ◽  
2014 ◽  
Vol 45 (16) ◽  
pp. no-no
Author(s):  
Markus Mansueto ◽  
Wolfgang Frey ◽  
Sabine Laschat

Giant ◽  
2021 ◽  
pp. 100088
Author(s):  
Shanju Zhang ◽  
Evan Beach ◽  
Paul T. Anastas ◽  
Lisa D. Pfefferle ◽  
Chinedum O. Osuji

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. . The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.


2010 ◽  
Vol 16 (15) ◽  
pp. 4588-4601 ◽  
Author(s):  
Xiaohong Cheng ◽  
Xueqing Bai ◽  
Shan Jing ◽  
Helgard Ebert ◽  
Marko Prehm ◽  
...  

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