A Comparative Study of the Phase Separation of a Nematic Liquid Crystal in the Self-assembling Drying Protein Drops

MRS Advances ◽  
2019 ◽  
Vol 4 (22) ◽  
pp. 1309-1314 ◽  
Author(s):  
Anusuya Pal ◽  
Amalesh Gope ◽  
Germano S. Iannacchione
Keyword(s):  
Liquid Crystal ◽  
Phase Separation ◽  
Self Assembly ◽  
Intensity Variation ◽  
The Self ◽  
Drying Process ◽  
Bright Region ◽  
Self Assembling ◽  
Initial Aqueous Solution ◽  
Significant Difference

ABSTRACTThe drying process, self-assembly of the proteins and the phase separation of a thermotropic liquid crystal (LC) from an initial aqueous solution represent a rich area of study. A focus of this work is to compare the behavior of two different proteins, bovine serum albumin [BSA] and lysozyme [Lys] in the ternary system through optical microscopy. During the drying process, the intensity profile shows three regimes in the presence of LC whereas no intensity variation is observed in its absence in both protein drops. The striking outcome is the presence of an umbilical defect of [+1] strength in every domain near the edge of BSA drop, whereas, each domain has a central dark region surrounded by a bright region in the dried Lys drop. Finally, the crack spacing in the dried Lys drop is reduced in the presence of LC whereas, no significant difference is found in the dried BSA drop.

Phase separation of a nematic liquid crystal in the self-assembly of lysozyme in a drying aqueous solution drop

2019 ◽  
Vol 9 (01) ◽  
pp. 150-158 ◽  
Author(s):  
Anusuya Pal ◽  
Amalesh Gope ◽  
Rumani Kafle ◽  
Germano S. Iannacchione
Keyword(s):  
Aqueous Solution ◽  
Liquid Crystal ◽  
Phase Separation ◽  
Nematic Liquid Crystal ◽  
Self Assembly ◽  
The Self ◽  
Image Position

Abstract

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 Optical Response Associated with the Orientation and Structure of Liquid Crystals with Respect to Phosphatidylcholine Concentration

Crystals ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 678
Author(s):  
Yuqi Han ◽  
Yan Jiang ◽  
Wei Guo ◽  
Bing Li ◽  
Lu Zhang ◽  
...  
Keyword(s):  
Liquid Crystal ◽  
Liquid Crystals ◽  
Reflectance Spectrum ◽  
Optical Response ◽  
The Self ◽  
Cholesteric Liquid Crystals ◽  
Anchoring Effect ◽  
Self Assembling ◽  
Sensitization Effect ◽  
Structure Of Liquid

Based on the anchoring effect due to the self-assembling behavior of the phospholipid molecules at the interface between the liquid crystal and water phases on the orientation of liquid crystals, the optical response associated with the orientation and structure of liquid crystals with respect to the concentration of 1,2-didodecanoyl-sn-glycero-3-phosphocholine solution has been investigated. The optical response owing to changes in the orientation and structure of the mixed cholesteric liquid crystals with respect to the change in the concentration of phosphatidylcholine has been obtained. Moreover, the feasibility of using as-prepared mixed cholesteric liquid crystals to measure the phosphatidylcholine concentration has been verified. A methodology to measure the reflectance spectrum by using mixed cholesteric liquid crystals to sensitize the phosphatidylcholine concentration has been further realized. The sensitization effect of the mixed cholesteric liquid crystals on the measurement of phosphatidylcholine concentration was also verified.

A Biological System Producing a Self-Assembling Cholesteric Protein Liquid Crystal

1971 ◽  
Vol 8 (1) ◽  
pp. 93-109
Author(s):  
A. C. NEVILLE ◽  
B. M. LUKE
Keyword(s):  
Liquid Crystal ◽  
Electron Density ◽  
Electron Micrographs ◽  
Self Assembly ◽  
Liquid Crystalline ◽  
Density Variation ◽  
Self Assembling ◽  
The Matrix ◽  
Electron Density Variation ◽  
Helicoidal Structure

The protein in the oothecal glands of praying mantids (Sphodromantis tenuidentata, Miomantis monacha) exists in the form of lamellar liquid crystalline spherulites, which coalesce as they flow out of a punctured gland tubule. Electron micrographs of sections of these spherulites after fixation show parabolic patterns of an electron-light component, set in a continuous matrix of protein. Such patterns arise in helicoidal systems (e.g. arthropod cuticle) and microdensitometric scans of the matrix show a rhythmical electron-density variation consistent with helicoidal structure. Double spiral patterns identical to those seen in liquid crystal spherulites are illustrated. These properties resemble those of cholesteric liquid crystals. The constructional units appear to be molecular rather than fibrillar as described by previous authors. The helicoidal architecture arises by self-assembly in the gland lumen. Lamellar surface structures self-assembled spontaneously on glass coverslips when the protein was left to stand for several days. When heated to 55 °C, the birefringent liquid crystalline protein abruptly changes to an isotropic gel, with associated loss of parabolic patterning in electron micrographs and of the rhythmical electron-density variation on microdensitometric scans. This behaviour is compared to the formation of gelatin from collagen, in terms of the randomization of an originally ordered secondary structure.

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>

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-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

scholarly journals 2-Deoxyglucose-Modified Folate Derivative: Self-Assembling Nanoparticle Able to Load Cisplatin

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1084 ◽  
Author(s):  
Shaoming Jin ◽  
Zhongyao Du ◽  
Pengjie Wang ◽  
Huiyuan Guo ◽  
Hao Zhang ◽  
...  
Keyword(s):  
Folic Acid ◽  
Self Assembly ◽  
Water Solubility ◽  
Pure Water ◽  
The Self ◽  
Molar Ratio ◽  
Antineoplastic Drugs ◽  
Self Assembling ◽  
Bonding Interaction ◽  
Nano Drug Delivery

Folic acid has been widely introduced into nano-drug delivery systems to give nanoparticle-targeted characteristics. However, the poor water solubility of folic acid may hinder the exploitation of its ability to load antineoplastic drugs. In the present study, we designed a new folate derivative (FA-2-DG) synthesized from folic acid and 2-Deoxyglucose (2-DG). The aim of this study was to evaluate the self-assembly characteristics of FA-2-DG, and its ability of loading cisplatin. The critical micelle concentration was 7.94 × 10−6 mol L−1. Fourier transform infrared spectroscopy indicated that hydrogen bonding interaction is a main driving force for the self–assembly of FA-2-DG. The particle was stable in pure water or 0.5% bovine serum albumin dispersions. By forming a coordination bond, the particles assembled from FA-2-DG can load cisplatin. The loading efficiency was maximal when the molar ratio of FA-2-DG to cisplatin was 2:1.

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