Self-Assembling Functionalized Amino Acids into Unusual Shapes

2011 ◽  
Vol 1312 ◽  
Author(s):  
Justin R. Barone ◽  
Naresh K. Budhavaram ◽  
Katherine J. Harvey

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.

2021 ◽  
Author(s):  
Bharti Koshti ◽  
Ramesh Singh ◽  
Vivekshinh Kshtriya ◽  
Shanka Walia ◽  
Dhiraj Bhatia ◽  
...  

<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>


2013 ◽  
Vol 834-836 ◽  
pp. 450-453
Author(s):  
Han Feng Cui ◽  
Yan Lin ◽  
Hao Fan ◽  
Li De Yu ◽  
Ping Nan Wan

Double conjugate addition of thiols with dienones was catalyzed by amino acids at room temperature in methanol, to afford the corresponding addition product in good to excellent yields.


1968 ◽  
Vol 14 (10) ◽  
pp. 967-978 ◽  
Author(s):  
Harold H Brown

Abstract The reaction of 2,4,6-trinitrobenzenesulfonic acid (TNBS) with amino acids was investigated by a static system to develop optimum conditions for application to automated amino acid chromatography. TNBS was found to be a very simple and sensitive reagent, easier to use than ninhydrin. The reaction occurs quite rapidly at room temperature, eliminating the requirement of a heating bath. The major disadvantage is a much lower sensitivity to the imino acid proline than to the amino acids.


Blood ◽  
1975 ◽  
Vol 45 (1) ◽  
pp. 45-48 ◽  
Author(s):  
NM Rumen

Abstract Sickling of erythrocytes was rapidly and quantitatively inhibited at room temperature by 3.8 mM homoserine, asparagine, and glutamine but by no other amino acid.


Clay Minerals ◽  
1992 ◽  
Vol 27 (1) ◽  
pp. 109-118 ◽  
Author(s):  
B. Siffert ◽  
A. Naidja

AbstractOptical isomers deamination of L- and D-glutamic and aspartic amino acids and of their DL racemic mixtures has been achieved in the presence of Na-montmorillonite at pH = 6 and room temperature. The adsorption curves showed that the enantiomer adsorbed depends on the type of amino acid. Nevertheless, deamination reaction kinetics brought about a stereoselectivity of the clay mineral for the L-isomer and implicitly showed an unquestionable “structural chirality character” of the clay mineral.


RSC Advances ◽  
2016 ◽  
Vol 6 (40) ◽  
pp. 33686-33694 ◽  
Author(s):  
P. R. Deepthi ◽  
J. Shanthi

Pure TGS and amino acid (l-arginine, l-histidine and l-alanine) doped TGS crystals were grown by a slow evaporation solution growth technique at room temperature.


1977 ◽  
Vol 55 (5) ◽  
pp. 906-910 ◽  
Author(s):  
S. T. Cheung ◽  
N. Leo Benoiton

The preparation of enantiomerically pure N-tert-butyloxycarbonyl,N-methylamino acids by N-methylation of the parent amino acid derivatives using sodium hydride and methyl iodide in tetrahydrofuran at room temperature is described for neutral amino acids including O-benzyl-protected threonine and tyrosine. Methylation of the O-benzylserine derivative under these conditions gives the N-methyldehydroalanine derivative. The β-elimination is completely suppressed, giving the corresponding N-methylserine derivative when the reaction is carried out at 5 °C. Other related data on N-methylation and N-methylamino acid derivatives are presented.


DICP ◽  
1989 ◽  
Vol 23 (10_suppl) ◽  
pp. S44-S46
Author(s):  
Linda S. Bullock

The use of histamine2-receptor antagonists could be beneficial in critically ill patients for protection against stress-induced gastrointestinal bleeding. Famotidine, similar to cimetidine and ranitidine, is stable when mixed in dextrose 5% injection and NaCl 0.9% injection at a concentration of 200 μg/mL and stored in polyvinyl chloride bags at 4 °C for 14 days or when frozen for 28 days and subsequently refrigerated for 14 days. Furthermore, famotidine, also like cimetidine and ranitidine, is stable when added to most common total parenteral nutrition (TPN) solutions. Famotidine in concentrations of 20 mg/L and 40 mg/L is stable in crystalline amino acid solutions (20 g/L and 42.5 g/L) when refrigerated for 24 hours, then held at room temperature for 24 hours, at room temperature for 48 hours, or refrigerated for seven days. The concentration of amino acids in the TPN solutions containing 42.5 g/L also is not affected by the addition of famotidine 40 mg/L when stored under conditions similar to those stated above for 48 hours. TPN solutions remain clear and free of turbidity.


2021 ◽  
Author(s):  
Bharti Koshti ◽  
Ramesh Singh ◽  
Vivekshinh Kshtriya ◽  
Shanka Walia ◽  
Dhiraj Bhatia ◽  
...  

<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>


1974 ◽  
Vol 27 (9) ◽  
pp. 2047 ◽  
Author(s):  
B Halpern ◽  
AP Hope

Condensates of some 2-hydroxyaryl ketones with protein amino acids have been prepared. The reaction has been shown to proceed without racemization and the derivatives have been isolated as free acids. Their unusual stability is ascribed to the presence of a strong intramolecular hydrogen bond. The N-arylmethylene function is cleaved under mild conditions of acid hydrolysis. Ketimines derived from D-phenylglycine decarboxylate at room temperature.


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