Concentration dependent morphological transition of nanostructured self-assembly towards hydrogelation seeding from micellar aggregates through stereochemically optimized H-bonding network of amino acid derived cationic amphiphiles

Author(s):  
Saubhik Haldar ◽  
Koninika Karmakar
2015 ◽  
Vol 6 (34) ◽  
pp. 6152-6162 ◽  
Author(s):  
Kamal Bauri ◽  
Amal Narayanan ◽  
Ujjal Haldar ◽  
Priyadarsi De

Amino acid coated chiral nanostructured soft materials are made by the polymerization induced self-assembly (PISA) technique, where the post-polymerization chemical group transformation leads to a morphological transition.


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.


Soft Matter ◽  
2020 ◽  
Vol 16 (28) ◽  
pp. 6599-6607 ◽  
Author(s):  
Pijush Singh ◽  
Souvik Misra ◽  
Nayim Sepay ◽  
Sanjoy Mondal ◽  
Debes Ray ◽  
...  

The self-assembly and photophysical properties of 4-nitrophenylalanine (4NP) are changed with the alteration of solvent and final self-assembly state of 4NP in competitive solvent mixture and are dictated by the solvent ratio.


2017 ◽  
Vol 70 (2) ◽  
pp. 126 ◽  
Author(s):  
Mark P. Del Borgo ◽  
Ketav Kulkarni ◽  
Marie-Isabel Aguilar

The unique structures formed by β-amino acid oligomers, or β-peptide foldamers, have been studied for almost two decades, which has led to the discovery of several distinctive structures and bioactive molecules. Recently, this area of research has expanded from conventional peptide drug design to the formation of assemblies and nanomaterials by peptide self-assembly. The unique structures formed by β-peptides give rise to a set of new materials with altered properties that differ from conventional peptide-based materials; such new materials may be useful in several bio- and nanomaterial applications.


2006 ◽  
pp. 4847-4849 ◽  
Author(s):  
Bulusu Jagannadh ◽  
Marepally Srinivasa Reddy ◽  
Chennamaneni Lohitha Rao ◽  
Anabathula Prabhakar ◽  
Bharatam Jagadeesh ◽  
...  

Biologia ◽  
2007 ◽  
Vol 62 (4) ◽  
Author(s):  
Reda Sammour

AbstractThe main goal of this work was to make the cDNA-encoding subunit G2 of soybean glycinin, capable of self-assembly in vitro and rich in methionine residues. Two mutants (pSP65/G4SacG2 and pSP65/G4SacG2HG4) were therefore constructed. The constructed mutants were successfully assembled in vitro into oligomers similar to those occurred in the seed. The successful self-assembly was due to the introduction of Sac fragment of Gy4 (the codons of the first 21 amino acid residues), which reported to be the key element in self-assembly into trimers. The mutant pSP65/G4SacG2HG4 included the acidic chain of Gy4 (HG4), which was previously molecularly modified to have three methionine residues. This mutant will be useful in the efforts to improve the seed quality.


2008 ◽  
Vol 319 (2) ◽  
pp. 526-533 ◽  
Author(s):  
Mariana Gerova ◽  
Fernanda Rodrigues ◽  
Jean-François Lamère ◽  
Alexander Dobrev ◽  
Suzanne Fery-Forgues

2017 ◽  
Vol 7 (6) ◽  
pp. 20160099 ◽  
Author(s):  
Wathsala Liyanage ◽  
Paul W. Rubeo ◽  
Bradley L. Nilsson

Peptide and low molecular weight amino acid-based materials that self-assemble in response to environmental triggers are highly desirable candidates in forming functional materials with tunable biophysical properties. In this paper, we explore redox-sensitive self-assembly of cationic phenylalanine derivatives conjugated to naphthalene diimide (NDI). Self-assembly of the cationic Phe-NDI conjugates into nanofibrils was induced in aqueous solvent at high ionic strength. Under reducing conditions, these self-assembled Phe-NDI conjugate fibrils underwent a morphological change to non-fibril aggregates. Upon reoxidation, the initially observed fibrils were reformed. The study herein provides an interesting strategy to effect reversible switching of the structure of supramolecular materials that can be applied to the development of sophisticated stimulus-responsive materials.


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