Assembly of amino acid containing naphthalene diimide-based molecules: the role of intervening amide groups in self-assembly, gelation, optical and semiconducting properties

Soft Matter ◽  
2019 ◽  
Vol 15 (14) ◽  
pp. 3018-3026 ◽  
Author(s):  
Nibedita Nandi ◽  
Kousik Gayen ◽  
Arindam Banerjee
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Naphthalene Diimide ◽  
Semiconducting Properties

Two isomeric amino-acid containing naphthalene diimide based molecules differ in their respective assembly and the intervening amide groups plays an important role in gelation, optical and semiconducting nature of these molecules.

scholarly journals Redox-sensitive reversible self-assembly of amino acid–naphthalene diimide conjugates

2017 ◽  
Vol 7 (6) ◽  
pp. 20160099 ◽  
Author(s):  
Wathsala Liyanage ◽  
Paul W. Rubeo ◽  
Bradley L. Nilsson
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Functional Materials ◽  
Supramolecular Materials ◽  
Responsive Materials ◽  
Naphthalene Diimide ◽  
Reducing Conditions ◽  
Aqueous Solvent ◽  
Stimulus Responsive ◽  
Fibril Aggregates

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.

Mimicking the Function of Eggshell Matrix Proteins: The Role of Multiplets of Charged Amino Acid Residues and Self-Assembly of Peptides in Biomineralization

2005 ◽  
Vol 44 (34) ◽  
pp. 5476-5479 ◽  
Author(s):  
Parayil Kumaran Ajikumar ◽  
Subramanian Vivekanandan ◽  
Rajamani Lakshminarayanan ◽  
Seetharama D. S. Jois ◽  
R. Manjunatha Kini ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Matrix Proteins ◽  
Amino Acid Residues ◽  
Eggshell Matrix

Understanding the Role of H-Bonding in Aqueous Self-Assembly of Two Naphthalene Diimide (NDI)-Conjugated Amphiphiles

Langmuir ◽  
2014 ◽  
Vol 30 (8) ◽  
pp. 1969-1976 ◽  
Author(s):  
Priya Rajdev ◽  
Mijanur Rahaman Molla ◽  
Suhrit Ghosh
Keyword(s):  
Self Assembly ◽  
Naphthalene Diimide

scholarly journals Self-organization of amino-acid-derived NDI assemblies into a nanofibrillar superstructure with humidity sensitive n-type semiconducting properties

2017 ◽  
Vol 53 (70) ◽  
pp. 9713-9716 ◽  
Author(s):  
Marco A. Squillaci ◽  
Grzegorz Markiewicz ◽  
Anna Walczak ◽  
Artur Ciesielski ◽  
Artur R. Stefankiewicz ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Amino Acid ◽  
Solid State ◽  
Nmr Spectroscopy ◽  
Self Assembly ◽  
Self Organization ◽  
Force Microscopy ◽  
Atomic Force ◽  
Semiconducting Properties

The hierarchical self-assembly of l-tyrosine substituted naphthalenediimide has been explored in solution by NMR spectroscopy and in the solid-state by atomic force microscopy.

Mimicking the Function of Eggshell Matrix Proteins: The Role of Multiplets of Charged Amino Acid Residues and Self-Assembly of Peptides in Biomineralization

2005 ◽  
Vol 117 (34) ◽  
pp. 5612-5615 ◽  
Author(s):  
Parayil Kumaran Ajikumar ◽  
Subramanian Vivekanandan ◽  
Rajamani Lakshminarayanan ◽  
Seetharama D. S. Jois ◽  
R. Manjunatha Kini ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Matrix Proteins ◽  
Amino Acid Residues ◽  
Eggshell Matrix

scholarly journals Unravelling the role of amino acid sequence order in the assembly and function of the amyloid-β core

2019 ◽  
Vol 55 (59) ◽  
pp. 8595-8598 ◽  
Author(s):  
Santu Bera ◽  
Elad Arad ◽  
Lee Schnaider ◽  
Shira Shaham-Niv ◽  
Valeria Castelletto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Self Assembly ◽  
Amyloid Β ◽  
The Self ◽  
Biological Functions ◽  
The Core ◽  
Recognition Motif ◽  
And Function

Here we report the influence of amino acid sequence order on the self-assembly and biological functions of the core recognition motif of Amyloid β.

Role of amino acid hydrophobicity, aromaticity, and molecular volume on IAPP(20-29) amyloid self-assembly

2012 ◽  
Vol 80 (4) ◽  
pp. 1053-1065 ◽  
Author(s):  
Todd M. Doran ◽  
Alissa J. Kamens ◽  
Nadia K. Byrnes ◽  
Bradley L. Nilsson
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Molecular Volume

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.

Sign in / Sign up

Export Citation Format

Share Document