scholarly journals Investigating the Effects of Aromatic Amino Acids on Amphipathic Peptide Self-Assembly and Emergent Hydrogel Viscoelasticity

2015 ◽  
Author(s):  
Annada Rajbhandary ◽  
Bradley L. Nilsson
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Amphipathic Peptide

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

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.

Self-assembly of aromatic amino acids: a molecular dynamics study

2018 ◽  
Vol 20 (48) ◽  
pp. 30525-30536 ◽  
Author(s):  
Sahin Uyaver ◽  
Helen W. Hernandez ◽  
M. Gokhan Habiboglu
Keyword(s):  
Molecular Dynamics ◽  
Amino Acids ◽  
Self Assembly ◽  
Aromatic Amino Acids

Common structures identified in the assembly of aromatic amino acids and their mixtures include the four-fold tube (a and b) and the zig-zag structure (c and d).

Self-Assembly Evolution of N-Terminal Aromatic Amino Acids with Transient Supramolecular Chirality

2020 ◽  
Vol 11 (4) ◽  
pp. 1490-1496 ◽  
Author(s):  
Shixin Xue ◽  
Nan Zhang ◽  
Xiaoling Hu ◽  
Yongfei Zeng ◽  
Jingbo Zhang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Supramolecular Chirality

scholarly journals Controlled self-assembly of modified aromatic amino acids

2021 ◽  
Author(s):  
Nidhi Gour ◽  
Vivekshinh Kshtriya ◽  
Bharti Koshti ◽  
Hanuman Narode ◽  
Soumick Naskar
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Aromatic Amino Acids

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

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.

scholarly journals Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
First Report ◽  
First Time

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.

scholarly journals Controlled self-assembly of modified aromatic amino acids

2021 ◽  
Author(s):  
Nidhi Gour ◽  
Vivekshinh Kshtriya ◽  
Bharti Koshti ◽  
Hanuman Narode ◽  
Soumick Naskar
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Aromatic Amino Acids

scholarly journals Designing a Transparent and Fluorine Containing Hydrogel

Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 43
Author(s):  
Paolo Ravarino ◽  
Demetra Giuri ◽  
Davide Faccio ◽  
Claudia Tomasini
Keyword(s):  
Amino Acids ◽  
Small Molecules ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Halogen Bonds ◽  
Aromatic Rings ◽  
Small Peptides ◽  
Supramolecular Materials ◽  
Fluorinated Amino Acids ◽  
Additional Formation

Physical hydrogels are supramolecular materials obtained by self-assembly of small molecules called gelators. Aromatic amino acids and small peptides containing aromatic rings are good candidates as gelators due to their ability to form weak bonds as π-π interactions and hydrogen bonds between NH and CO of the peptide chain. In this paper we show our results in the preparation of a transparent hydrogel that was obtained by self-assembly of a fluorine-containing dipeptide that relies on the additional formation of halogen bonds due to the fluorine atoms contained in the dipeptide. We used Boc-D-F2Phe-L-Oxd-OH (F2Phe = 3,4-difluorophenylalainine; Oxd = 4-methyl-5-carboxy-oxazolidin-2-one) that formed a strong and transparent hydrogel in 0.5% w/w concentration at pH = 4.2. The formation of a hydrogel made of unnatural fluorinated amino acids may be of great interest in the evaluation of patients with parkinsonian syndromes and may be used for controlled release.

scholarly journals SAPdb: A database of nanostructures formed by self-assembly of short peptides

2019 ◽  
Author(s):  
Deepika Mathur ◽  
Harpreet Kaur ◽  
Anjali Dhall ◽  
Neelam Sharma ◽  
Gajendra P. S. Raghava
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
The Self ◽  
Single Amino Acid ◽  
Short Peptides ◽  
Experimental Conditions ◽  
Surface Receptors ◽  
Self Assembling ◽  
Comprehensive Information

AbstractBackgroundNanostructures generated by self-assembly of peptides yield nanomaterial that has many therapeutic applications, including drug delivery and biomedical engineering, due to their low cytotoxicity and higher uptake by targeted cells owing to their high affinity and specificity towards cell surface receptors. Despite the promising implications of this rapidly expanding field, there is no dedicated resource to study peptide nanostructures.ResultThis study endeavours to create a dedicated repository of short peptides, which may prove to be the best models to study ordered nanostructures formed by peptide self-assembly. SAPdb has a repertoire of 1,049 entries of experimentally validated nanostructures formed by the self-assembling of small peptides. It includes 701 entries are of dipeptides, 328 entries belong to tripeptides, and 20 entries of single amino acid with some conjugated partners. Each entry encompasses comprehensive information about the peptide such as chemical modifications in the peptide sequences, the type of nanostructure formed, and experimental conditions like pH, temperature, and solvent required for the self-assembly of the peptide, etc. Further, our analysis has shown that the occurrence of aromatic amino acids favours the formation of self-assembling nanostructures, as indicated by a large number of entries in SAPdb contain aromatics amino acids. Besides, we have observed that these peptides form different nanostructures under different experimental conditions. SAPdb provides this comprehensive information in a hassle-free tabulated manner at a glance. User-friendly browsing, searching, and analysis modules are integrated for easy retrieval and comparison of data and examination of properties. We anticipate SAPdb to be a valuable repository for researchers engaged in the burgeoning arena of nanobiotechnology.AvailabilityThe database can be accessed on the web at https://webs.iiitd.edu.in/raghava/sapdb.

Sign in / Sign up

Export Citation Format

Share Document