pH-Responsive self-assembly in an aqueous mixture of surfactant and hydrophobic amino acid mimic

Soft Matter ◽  
2009 ◽  
Vol 5 (15) ◽  
pp. 2919 ◽  
Author(s):  
Gunjan Verma ◽  
Vinod Kumar Aswal ◽  
Puthusserickal Hassan
Langmuir ◽  
2014 ◽  
Vol 30 (38) ◽  
pp. 11307-11318 ◽  
Author(s):  
Anna Bogomolova ◽  
Sandro Keller ◽  
Johannes Klingler ◽  
Marian Sedlak ◽  
Dmytro Rak ◽  
...  

Biomaterials ◽  
2009 ◽  
Vol 30 (10) ◽  
pp. 1954-1961 ◽  
Author(s):  
Rongjun Chen ◽  
Sariah Khormaee ◽  
Mark E. Eccleston ◽  
Nigel K.H. Slater

2009 ◽  
Vol 19 (24) ◽  
pp. 4217 ◽  
Author(s):  
Rongjun Chen ◽  
Mark E. Eccleston ◽  
Zhilian Yue ◽  
Nigel K. H. Slater

Langmuir ◽  
2013 ◽  
Vol 29 (8) ◽  
pp. 2764-2774 ◽  
Author(s):  
Kamal Bauri ◽  
Saswati Ghosh Roy ◽  
Shashank Pant ◽  
Priyadarsi De

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 ◽  
...  

Author(s):  
Wei He ◽  
Wenhui Zhang ◽  
Zhenhua Chu ◽  
Yu Li

The aim of this paper is to explore the mechanism of the change in oestrogenic activity of PCBs molecules before and after modification by designing new PCBs derivatives in combination with molecular docking techniques through the constructed model of oestrogenic activity of PCBs molecules. We found that the weakened hydrophobic interaction between the hydrophobic amino acid residues and hydrophobic substituents at the binding site of PCB derivatives and human oestrogen receptor alpha (hERα) was the main reason for the weakened binding force and reduced anti-oestrogenic activity. It was consistent with the information that the hydrophobic field displayed by the 3D contour maps in the constructed oestrogen activity CoMSIA model was one of the main influencing force fields. The hydrophobic interaction between PCB derivatives and oestrogen-active receptors was negatively correlated with the average distance between hydrophobic substituents and hydrophobic amino acid residues at the hERα-binding site, and positively correlated with the number of hydrophobic amino acid residues. In other words, the smaller the average distance between the hydrophobic amino acid residues at the binding sites between the two and the more the number of them, and the stronger the oestrogen activity expression degree of PCBS derivative molecules. Therefore, hydrophobic interactions between PCB derivatives and the oestrogen receptor can be reduced by altering the microenvironmental conditions in humans. This reduces the ability of PCB derivatives to bind to the oestrogen receptor and can effectively modulate the risk of residual PCB derivatives to produce oestrogenic activity in humans.


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.


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