Sequential and cellular detection of copper and lactic acid by disaggregation and reaggregation of the fluorescent panchromatic fibres of an acylthiourea based sensor

Koshti

Naskar

et al. 2021

Preprint

Self Cite

Herein, we report the self-assembled structure formed by Fmoc protected charge single amino acid Fmoc-L-glutamic acid 5-tert-butyl ester (Fmoc-Glu(OtBu)-OH), Fmoc-Laspartic acid 4-tert-butyl ester (Fmoc-Asp(OtBu)-OH), and Na-Fmoc-Ne-Boc-L-lysine (Fmoc-Lys(Boc)-OH). The self-assembled architecture formed by the charge aliphatic amino acids were assessed under different conditions such as concentration, temperature and pH.Fmoc-Glu(OtBu)-OH assembled to spheres at both lower and higher concentration under room temperature condition. However, it forms a broom stick like morphology at both lower and higher concentration on heating. Fmoc-Asp(OtBu)-OH on the other hand formed rod like at both both low and high concentration and also on hhealing. Fmoc-Lys(Boc)-OH also self-assemble to sphere like morphology in all conditions irrespective of concentration and heating. Since these structure are very intriguing, our future endevorous is to study these structure through different microscopic techniques such as scanning electron microscopy (SEM), Transmission Electron microscopy (TEM). The mechanisms of the structure formation by these amino acids will be characterized by using solution state NMR, FTIR and TGA in future. The self-assembled structures formed by modified amino acids are easy and facile route to design novel nanoarchitectures which may be potentially useful in future for various type of applications in the field of material chemistry, bioscience, biomedical.

Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Controlled aggregation properties of modified single amino acids

Koshti

Naskar

et al. 2021

Preprint

Self Cite

“…32 In another study mechanical properties of Fmocdiphenylalanine were studied 33 and also the self-assembly of Fmoc-peptides was used for the preparation of nanostructures and hydrogels, 34 Our group has been interested in assessing the self-assembling properties of single amino acids, 3,35 peptides, [36][37][38] and heterocyclic compounds. 10,[38][39][40][41][42] Recently, we reported selfassembled structure formation of cysteine and methionine and its amyloid like characteristic. 3 In other study our group has also reported the self-assembled structure formed by proline, hydroxyproline 35 and lysine.HCl.…”

Section: Introductionmentioning

confidence: 99%

Controlled Morphological Changes in Self-Assembled Structures Formed by Fmoc Variants of Threonine and Serine

Kshtriya¹,

Koshti²,

2021

Preprint

Self Cite

We report for the very first time the self-assembly of<a> </a>Fmoc variant 2-(9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(tert-butoxy)butanoic acid of threonine (Fmoc-Thr(tbu)-OH) and <a>of serine (</a>Fmoc-Ser(tbu)-OH. The self-assembled structure formation of Fmoc variants of threonine and serine were examined under varying concentration and temperature conditions..Our studies reveal that the self-assembled structures formed by Fmoc-Thr(tbu)-OH and Fmoc-Ser(tbu)-OH reveal morphological transitions at the supramolecular level as we alter its concentration and temperature. Fmoc-Thr(tbu)-OH self-assembles to sphere at lower concentration which changes to dumb-bell shapes at higher concentration under room temperature conditions. When the solution at lower concentration is heated the spheres changes to rods while the dumb bell shapes at higher concentrations change to elongated dumb-bell-rod like morphologies. Fmoc-Ser(tbu)-OH on the other hand give flower like morphologies at lower concentration which changes to long rods at higher concentration. On heating at higher temperature 70 οC flower-like structures change to small rods while the long rods obtained at higher concentration changes to big flower-like structures. The controlled morphological changes noted in the modified single amino acids is very interesting and pave the way for the design of novel self-assembled architectures for applications in material science and nanotechnology.

“…Since our group has been working on the molecular self-assembly and assessing the selfassembly of the single amino acids, 8,9,17,18 modified single amino acids, 19 peptides, [20][21][22][23][24][25][26] nanoparticle/nanomaterial, [27][28][29] and heterocyclic [30][31][32][33][34][35] compounds. Our group reported for the very first time the amyloid-like self-assembled structure formed by the non-aromatic single amino acid cysteine and methionine 8 .…”

Section: Introductionmentioning

confidence: 99%

Controlled self-assembly of modified aromatic amino acids

Kshtriya

Koshti

et al. 2021

Preprint

Self Cite

We report the self-assembly of carbobenzoxyphenylalanine (Z-Phe-OH), carbobenzoxytryptophan (Z-Trp-OH), carbobenzoxytyrosine (Z-Tyr-OH) and N-(9-Fluorenylmethoxycarbonyl)-O-tert-butyl-L-tyrosine (Fmoc-Tyr(tbu)-OH) to well-defined morphologies such as fibers, spherical and flower-like self-assembled structure. The selfassembled structure formed by modify single amino acids were characterized through various microscopic and spectroscopic techniques. The self-assembled structure formation was studied extensively under varying concentrations and temperature and the mechanism of selfassembled structure formation was extensively studied through solution state 1 H NMR. The self-assembly studies on modified amino acid provide an important avenue for the simple fabrication and design of novel materials with immense applications. Hence, Z-Phe-OH, Z-Trp-OH, Z-Tyr-OH, and Fmoc-Tyr(tbu)-OH self-assembly studies may be a pertinent extension in this direction.