scholarly journals Poly(amino acid)-grafted polymacrolactones. Synthesis, self-assembling and ionic coupling properties

2019 ◽  
Vol 143 ◽  
pp. 104316 ◽  
Author(s):  
E. Tinajero-Díaz ◽  
A. Martínez de Ilarduya ◽  
B. Cavanagh ◽  
A. Heise ◽  
S. Muñoz-Guerra
Keyword(s):  
Amino Acid ◽  
Self Assembling ◽  
Ionic Coupling

Self-assembling behaviour of a modified aromatic amino acid in competitive medium

Soft Matter ◽  
2020 ◽  
Vol 16 (28) ◽  
pp. 6599-6607 ◽  
Author(s):  
Pijush Singh ◽  
Souvik Misra ◽  
Nayim Sepay ◽  
Sanjoy Mondal ◽  
Debes Ray ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acid ◽  
Photophysical Properties ◽  
Solvent Mixture ◽  
The Self ◽  
Solvent Ratio ◽  
Self Assembling

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.

scholarly journals Unusual Aggregation Properties of Single Amino Acid L-Lysine Hydrochloride

2021 ◽  
Author(s):  
Bharti Koshti ◽  
Ramesh Singh ◽  
Vivekshinh Kshtriya ◽  
Shanka Walia ◽  
Dhiraj Bhatia ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Short Term Memory ◽  
Deionized Water ◽  
The Body ◽  
The Self ◽  
Single Amino Acid ◽  
Maple Syrup ◽  
Self Assembling

<p>.<br></p><p>The self-assembly of single amino acids is very important topic of research since there are plethora of diseases like phenylketonuria, tyrosinemia, hypertryptophanemia, hyperglycinemia, cystinuria and maple syrup urine disease to name a few which are caused by the accumulation or excess of amino acids. These are in-born errors of metabolisms (IEM’s) which are caused due to the deficiency of enzymes involved in catabolic pathways of these enzymes. Hence, it is very pertinent to understand the fate of these excess amino acids in the body and their self-assembling behaviour at molecular level. From the previous literature reports it may be surmised that the single amino acids like Phenylalanine, Tyrosine, Tryptophan, Cysteine and Methionine assemble to amyloid like structures, and hence have important implications in the pathophysiology of IEM’s like phenylketonuria, tyrosinemia, hypertryptophanemia, cystinuria and hypermethioninemia respectively. In this manuscript we report the self-assembly of lysine hydrocholride to fiber like structures in deionized water. It could be observed that lysine assemble to globular structures in fresh condition and then gradually changes to fiber like morphologies by self-association over time after 24 hours. These fibers gradually change to tubular morphologies after 3 day followed by fractal irregular morphologies in 10 and 15 days respectively. Notably, lysine exists as positively charged amino acid at physiological pH and the amine groups in lysine remain protonated. Hence, the self-assembling properties of lysine hydrochloride in deionized water is also pertinent and give insights into the fate of this amino acid in body in case it remains unmetabolized. Further, MTT assays were done to analyse the toxicities of these aggregates and the assay suggest their cytotoxic nature on SHSY5Y neural cell lines. Hence, the aggregation of lysine may be attributed to the pathological symptoms caused in diseases like hyperlysinemia which is associated with the neurological problems like seizures and short-term memory as observed in case of amyloid diseases like Parkinson’s and Alzheimer’s to name a few.</p>

Self-Assembling Functionalized Amino Acids into Unusual Shapes

2011 ◽  
Vol 1312 ◽  
Author(s):  
Justin R. Barone ◽  
Naresh K. Budhavaram ◽  
Katherine J. Harvey
Keyword(s):  
Amino Acids ◽  
Hydrogen Bond ◽  
Amino Acid ◽  
Room Temperature ◽  
Vinyl Sulfone ◽  
Ethyl Vinyl ◽  
Simple Route ◽  
Self Assembling ◽  
Component Systems ◽  
Functionalized Amino Acids

ABSTRACTMulti-component small molecule systems that are amphiphilic or that can hydrogen bond end-to-end or side-to-side have been shown to self-assemble into a variety of shapes including fibers, rods, sheets, plates, spheres, and tubes. Recently, we have identified a simple route to self-assemble the same shapes from one-component systems. The structures form by attaching ethyl vinyl sulfone (EVS) to amino acids in water at room temperature. Choice of amino acid, amount of EVS substitution, and solvent conditions determine the final shape. Functionalized amino acids spontaneously form structures like fibers, spheres, tubes, and donuts when dried from solution. Here we focus on fibers and tubes.

Divalent Amino-Acid-Based Amphiphilic Antioxidants: Synthesis, Self-Assembling Properties, and Biological Evaluation

2016 ◽  
Vol 27 (3) ◽  
pp. 772-781 ◽  
Author(s):  
Marie Rosselin ◽  
Grégory Meyer ◽  
Pierre Guillet ◽  
Thomas Cheviet ◽  
Guillaume Walther ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Evaluation ◽  
Self Assembling

Novel Self-Assembling Amino Acid-Derived Block Copolymer with Changeable Polymer Backbone Structure

Langmuir ◽  
2016 ◽  
Vol 32 (47) ◽  
pp. 12378-12386 ◽  
Author(s):  
Tomoyuki Koga ◽  
Eri Aso ◽  
Nobuyuki Higashi
Keyword(s):  
Amino Acid ◽  
Block Copolymer ◽  
Polymer Backbone ◽  
Self Assembling ◽  
Backbone Structure

Influence of amino acid side chains on the formation of two component self-assembling nanofibrous hydrogels

2017 ◽  
Vol 41 (3) ◽  
pp. 1229-1234 ◽  
Author(s):  
Srinivasa Rao Nelli ◽  
Jhong-Hua Lin ◽  
Thi Ngoc Anh Nguyen ◽  
Dion Tzu-Huan Tseng ◽  
Satish Kumar Talloj ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Derivatives ◽  
Side Chains ◽  
Self Assembling ◽  
Two Component ◽  
Amino Acid Side Chains

Supramolecular co-assembly of amino acid derivatives capped with NDI and Py moieties undergoing supramolecular hydrogelation was developed.

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