scholarly journals Structural Dynamic of a Self-Assembling Peptide d-EAK16 Made of Only D-Amino Acids

PLoS ONE ◽  
2008 ◽  
Vol 3 (5) ◽  
pp. e2364 ◽  
Author(s):  
Zhongli Luo ◽  
Xiaojun Zhao ◽  
Shuguang Zhang
Keyword(s):  
Amino Acids ◽  
Structural Dynamic ◽  
Self Assembling

Directive Effect of Chain Length in Modulating Peptide Nano-assemblies

2020 ◽  
Vol 27 (9) ◽  
pp. 923-929
Author(s):  
Gaurav Pandey ◽  
Prem Prakash Das ◽  
Vibin Ramakrishnan
Keyword(s):  
Electron Microscopy ◽  
Amino Acids ◽  
Light Scattering ◽  
Chain Length ◽  
Self Assembly ◽  
The Self ◽  
Ionic Charge ◽  
Self Assembling ◽  
Biophysical Techniques

Background: RADA-4 (Ac-RADARADARADARADA-NH2) is the most extensively studied and marketed self-assembling peptide, forming hydrogel, used to create defined threedimensional microenvironments for cell culture applications. Objectives: In this work, we use various biophysical techniques to investigate the length dependency of RADA aggregation and assembly. Methods: We synthesized a series of RADA-N peptides, N ranging from 1 to 4, resulting in four peptides having 4, 8, 12, and 16 amino acids in their sequence. Through a combination of various biophysical methods including thioflavin T fluorescence assay, static right angle light scattering assay, Dynamic Light Scattering (DLS), electron microscopy, CD, and IR spectroscopy, we have examined the role of chain-length on the self-assembly of RADA peptide. Results: Our observations show that the aggregation of ionic, charge-complementary RADA motifcontaining peptides is length-dependent, with N less than 3 are not forming spontaneous selfassemblies. Conclusion: The six biophysical experiments discussed in this paper validate the significance of chain-length on the epitaxial growth of RADA peptide self-assembly.

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.

ChemInform Abstract: One-Pot Synthesis of Phenylseleno N-Acetyl α-Amino Acids: Supra-Molecular Self-Assembling in Organoselenium Compounds.

ChemInform ◽  
2014 ◽  
Vol 45 (15) ◽  
pp. no-no
Author(s):  
C. Parashiva Prabhu ◽  
Prasad P. Phadnis ◽  
Amey Wadawale ◽  
K. Indira Priyadarsini ◽  
Vimal K. Jain
Keyword(s):  
Amino Acids ◽  
Organoselenium Compounds ◽  
One Pot ◽  
One Pot Synthesis ◽  
Self Assembling

Self-Assembling Microspheres from Charged Functional Polyelectrolytes and Small-Molecule Counterions

2004 ◽  
Vol 823 ◽  
Author(s):  
Brandon Mckenna ◽  
Henrik Birkedal ◽  
Michael H. Bartl ◽  
Timothy J. Deming ◽  
Galen D. Stucky
Keyword(s):  
Amino Acids ◽  
Confocal Microscopy ◽  
Self Assembly ◽  
Fluorescent Labeling ◽  
Vesicle Formation ◽  
Assembly Process ◽  
Covalent Crosslinking ◽  
Self Assembling ◽  
Minimum Number ◽  
Sphere Formation

AbstractMicrometer-sized spheres have been found to assemble from homopolymer electrolytes and small, multivalent counterions in water. In contrast to previous efforts, these vesicles do not use preformed templates, do not require block copolymers, and do not necessarily employ nanoparticles. We have investigated the requirements for vesicle formation with regards to both components of the assembly. Self-assembly occurs with a variety of poly-amino acids and counterions, all of which require a minimum number of charged groups to promote non-covalent crosslinking. We show how the assembly process is controlled by pH and how, in consequence, the pKa's of the reactants can be used to reliably predict sphere formation. By varying the nature of the small counterions, we have determined the requirements for assemblies. The assemblies have been further investigated using confocal microscopy and fluorescent labeling of the different components.

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>

scholarly journals New self-assembling peptide nanotubes of large diameter using δ-amino acids

2018 ◽  
Vol 9 (43) ◽  
pp. 8228-8233 ◽  
Author(s):  
Alejandro Lamas ◽  
Arcadio Guerra ◽  
Manuel Amorín ◽  
Juan R. Granja
Keyword(s):  
Amino Acids ◽  
Building Block ◽  
Cyclic Peptides ◽  
Large Diameter ◽  
Peptide Nanotubes ◽  
Self Assembling ◽  
Aminocyclohexanecarboxylic Acid

Here we show that 4-aminocyclohexanecarboxylic acid is a rigid stretcher building block for the preparation of cyclic peptides that self-assemble to form peptide nanotubes with large diameter and hydrophobic pores.

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