scholarly journals Inulin nanostructures: The sweet-spot of carbohydrate self-assembly

2021 ◽  
Author(s):  
Zohar A. Arnon ◽  
Márkó Grabarics ◽  
Topaz Kreiser ◽  
Avi Raveh ◽  
Kevin Pagel ◽  
...  
Keyword(s):  
Nucleic Acids ◽  
Self Assembly ◽  
The Self ◽  
Dependent Manner ◽  
Supramolecular Architecture ◽  
Sweet Spot ◽  
Concentration Dependent Manner ◽  
Self Assembling ◽  
Spontaneous Organization

Supramolecular architecture formation by the self-assembly of proteins and nucleic acids is well studied. Yet, the spontaneous organization of oligosaccharides, the most common polymers in nature, is less explored. Here, using inulin as a model, we identify the "sweet spot" length for oligosaccharide assembly. Inulin forms discrete spheres in a concentration-dependent manner. Size-based fractionation displayed markedly different aggregation morphologies. Based on these findings, we believe that carbohydrates could become an important source for novel self-assembling materials.

Self-assembling triazolophanes: from croissants through donuts to spherical vesicles

2015 ◽  
Vol 51 (32) ◽  
pp. 6905-6908 ◽  
Author(s):  
V. Haridas ◽  
Appa Rao Sapala ◽  
Jerry P. Jasinski
Keyword(s):  
Crystal Structure ◽  
Self Assembly ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
X Ray ◽  
Self Assembling ◽  
Assembly Mechanism ◽  
Spherical Vesicles

A detailed ultramicroscopic analysis of three novel triazolophanes demonstrated a hierarchical self-assembly mechanism. These macrocycles self-assemble in a concentration dependent manner to hemi-toroids, toroids and finally to vesicles. The finding was supported by ultramicroscopy and X-ray crystal structure studies.

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.

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>

scholarly journals Biochemical reconstitutions reveal principles of human γ-TuRC assembly and function

2021 ◽  
Vol 220 (3) ◽  
Author(s):  
Michal Wieczorek ◽  
Shih-Chieh Ti ◽  
Linas Urnavicius ◽  
Kelly R. Molloy ◽  
Amol Aher ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Self Assembly ◽  
The Self ◽  
Dependent Manner ◽  
Guanine Nucleotide ◽  
Partial Cone ◽  
Ring Complex ◽  
Microtubule Networks ◽  
And Function

The formation of cellular microtubule networks is regulated by the γ-tubulin ring complex (γ-TuRC). This ∼2.3 MD assembly of &gt;31 proteins includes γ-tubulin and GCP2-6, as well as MZT1 and an actin-like protein in a “lumenal bridge” (LB). The challenge of reconstituting the γ-TuRC has limited dissections of its assembly and function. Here, we report a biochemical reconstitution of the human γ-TuRC (γ-TuRC-GFP) as a ∼35 S complex that nucleates microtubules in vitro. In addition, we generate a subcomplex, γ-TuRCΔLB-GFP, which lacks MZT1 and actin. We show that γ-TuRCΔLB-GFP nucleates microtubules in a guanine nucleotide–dependent manner and with similar efficiency as the holocomplex. Electron microscopy reveals that γ-TuRC-GFP resembles the native γ-TuRC architecture, while γ-TuRCΔLB-GFP adopts a partial cone shape presenting only 8–10 γ-tubulin subunits and lacks a well-ordered lumenal bridge. Our results show that the γ-TuRC can be reconstituted using a limited set of proteins and suggest that the LB facilitates the self-assembly of regulatory interfaces around a microtubule-nucleating “core” in the holocomplex.

Effect of H-bonding interactions of water molecules in the self assembly of supramolecular architecture-joint experimental and computational studies

2017 ◽  
Vol 1142 ◽  
pp. 148-155 ◽  
Author(s):  
Amanpreet Kaur Jassal ◽  
Rajwinder Kaur ◽  
Nasarul Islam ◽  
Anu ◽  
Rahul Kumar Mudsainiyan
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Water Molecules ◽  
Computational Studies ◽  
Supramolecular Architecture

scholarly journals Terminal short arm domains of basement membrane laminin are critical for its self-assembly.

1990 ◽  
Vol 110 (3) ◽  
pp. 825-832 ◽  
Author(s):  
J C Schittny ◽  
P D Yurchenco
Keyword(s):  
Self Assembly ◽  
Affinity Column ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Calcium Dependent ◽  
Domain Specific ◽  
Binding Domains ◽  
Individual Domain ◽  
The Individual

Laminin self-assembles into large polymers by a cooperative two-step calcium-dependent mechanism (Yurchenco, P. D., E. C. Tsilibary, A. S. Charonis, and H. Furthmayr. 1985. J. Biol. Chem. 260:7636-7644). The domain specificity of this process was investigated using defined proteolytically generated fragments corresponding to the NH2-terminal globule and adjacent stem of the short arm of the B1 chain (E4), a complex of the two short arms of the A and B2 chains attached to the proximal stem of a third short arm (E1'), a similar complex lacking the globular domains (P1'), and the distal half of the long arm attached to the adjacent portion of the large globule (E8). Polymerization, followed by an increase of turbidity at 360 nm in neutral isotonic TBS containing CaCl2 at 35 degrees C, was quantitatively inhibited in a concentration-dependent manner with laminin fragments E4 and E1' but not with fragments E8 and P1'. Affinity retardation chromatography was used for further characterization of the binding of laminin domains. The migration of fragment E4, but not of fragments E8 and P1', was retarded in a temperature- and calcium-dependent fashion on a laminin affinity column but not on a similar BSA column. These data are evidence that laminin fragments E4 and E1' possess essential terminal binding domains for the self-aggregation of laminin, while fragments E8 and P1' do not. Furthermore, the individual domain-specific interactions that contribute to assembly are calcium dependent and of low affinity.

The self-assembly and secondary structure of peptide amphiphiles determine the membrane permeation activity

RSC Advances ◽  
2014 ◽  
Vol 4 (58) ◽  
pp. 30654-30657 ◽  
Author(s):  
Rie Wakabayashi ◽  
Yuko Abe ◽  
Noriho Kamiya ◽  
Masahiro Goto
Keyword(s):  
Secondary Structure ◽  
Membrane Permeability ◽  
Self Assembly ◽  
The Self ◽  
Peptide Amphiphiles ◽  
Membrane Permeation ◽  
Related Peptide ◽  
Self Assembling

New GALA-related peptide amphiphiles were designed and the influence of their self-assembling propensity and the secondary structure on the membrane permeability was studied.

scholarly journals Self-Propulsion Enhances Polymerization

Entropy ◽  
2020 ◽  
Vol 22 (2) ◽  
pp. 251 ◽  
Author(s):  
Maximino Aldana ◽  
Miguel Fuentes-Cabrera ◽  
Martín Zumaya
Keyword(s):  
Nucleic Acids ◽  
Self Assembly ◽  
The Self ◽  
Biological Molecules ◽  
Bonding Energy ◽  
Self Organization ◽  
External Energy ◽  
Present Evidence ◽  
Spontaneous Process ◽  
Propulsion Force

Self-assembly is a spontaneous process through which macroscopic structures are formed from basic microscopic constituents (e.g., molecules or colloids). By contrast, the formation of large biological molecules inside the cell (such as proteins or nucleic acids) is a process more akin to self-organization than to self-assembly, as it requires a constant supply of external energy. Recent studies have tried to merge self-assembly with self-organization by analyzing the assembly of self-propelled (or active) colloid-like particles whose motion is driven by a permanent source of energy. Here we present evidence that points to the fact that self-propulsion considerably enhances the assembly of polymers: self-propelled molecules are found to assemble faster into polymer-like structures than non self-propelled ones. The average polymer length increases towards a maximum as the self-propulsion force increases. Beyond this maximum, the average polymer length decreases due to the competition between bonding energy and disruptive forces that result from collisions. The assembly of active molecules might have promoted the formation of large pre-biotic polymers that could be the precursors of the informational polymers we observe nowadays.

scholarly journals Self-assembly study of type I collagen extracted from male Wistar Hannover rat tail tendons

2020 ◽  
Vol 24 (1) ◽  
Author(s):  
Jeimmy González-Masís ◽  
Jorge M. Cubero-Sesin ◽  
Simón Guerrero ◽  
Sara González-Camacho ◽  
Yendry Regina Corrales-Ureña ◽  
...  
Keyword(s):  
Regenerative Medicine ◽  
Self Assembly ◽  
Type I Collagen ◽  
Ph Effect ◽  
The Self ◽  
Titration Calorimetry ◽  
Type I ◽  
Self Assembling ◽  
Functional Features ◽  
Rat Tail

Abstract Background Collagen, the most abundant protein in the animal kingdom, represents a promising biomaterial for regenerative medicine applications due to its structural diversity and self-assembling complexity. Despite collagen’s widely known structural and functional features, the thermodynamics behind its fibrillogenic self-assembling process is still to be fully understood. In this work we report on a series of spectroscopic, mechanical, morphological and thermodynamic characterizations of high purity type I collagen (with a D-pattern of 65 nm) extracted from Wistar Hannover rat tail. Our herein reported results can be of help to elucidate differences in self-assembly states of proteins using ITC to improve the design of energy responsive and dynamic materials for applications in tissue engineering and regenerative medicine. Methods Herein we report the systematic study on the self-assembling fibrillogenesis mechanism of type I collagen, we provide morphological and thermodynamic evidence associated to different self-assembly events using ITC titrations. We provide thorough characterization of the effect of pH, effect of salts and protein conformation on self-assembled collagen samples via several complementary biophysical techniques, including circular dichroism (CD), Fourier Transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), atomic force microscopy (AFM), scanning electron microscopy (SEM), dynamic mechanical thermal analysis (DMTA) and thermogravimetric analysis (TGA). Results Emphasis was made on the use of isothermal titration calorimetry (ITC) for the thermodynamic monitoring of fibrillogenesis stages of the protein. An overall self-assembly enthalpy value of 3.27 ± 0.85 J/mol was found. Different stages of the self-assembly mechanism were identified, initial stages take place at pH values lower than the protein isoelectric point (pI), however, higher energy release events were recorded at collagen’s pI. Denatured collagen employed as a control exhibited higher energy absorption at its pI, suggesting different energy exchange mechanisms as a consequence of different aggregation routes. Graphical abstract

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