scholarly journals Interfacial crystallization and supramolecular self-assembly of spider silk inspired protein at the water-air interface

2021 ◽  
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Assembly Process ◽  
Protein Solution ◽  
Time Resolved ◽  
Macromolecular Assembly ◽  
X Ray Scattering ◽  
Air Interface ◽  
Fundamental Research ◽  
Β Sheet

Abstract Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process we looked into highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water-air interface into a relatively thick and highly elastic skin. Using time-resolved in-situ synchrotron x-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid-liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

scholarly journals Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

Materials ◽  
2021 ◽  
Vol 14 (15) ◽  
pp. 4239
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Assembly Process ◽  
Protein Solution ◽  
Time Resolved ◽  
Macromolecular Assembly ◽  
X Ray Scattering ◽  
Air Interface ◽  
Fundamental Research ◽  
Β Sheet

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water–air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron X-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid–liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

scholarly journals Interfacial crystallization and supramolecular self-assembly of spider silk inspired protein at the water-air interface

2021 ◽  
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Assembly Process ◽  
Protein Solution ◽  
Time Resolved ◽  
Macromolecular Assembly ◽  
X Ray Scattering ◽  
Air Interface ◽  
Fundamental Research ◽  
Β Sheet

Abstract Abstract: Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process we looked into highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water-air interface into a relatively thick and highly elastic skin. Using time-resolved in-situ synchrotron x-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid-liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

2019 ◽  
Author(s):  
Hao Wu ◽  
Jeffrey Ting ◽  
Siqi Meng ◽  
Matthew Tirrell
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Electrostatic Interactions ◽  
Polyelectrolyte Complex ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Kinetics Of ◽  
Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

A lotus-inspired janus hybrid film enabled by interfacial self-assembly and in situ asymmetric modification

2018 ◽  
Vol 54 (91) ◽  
pp. 12804-12807 ◽  
Author(s):  
Yun Liang ◽  
Jiangwei Shi ◽  
Peng Xiao ◽  
Jiang He ◽  
Feng Ni ◽  
...  
Keyword(s):  
Self Assembly ◽  
Hybrid Film ◽  
Water Interface ◽  
Assembly Process ◽  
Lotus Leaf ◽  
Air Interface ◽  
Oil Water

A lotus leaf inspired Janus hybrid film was exquisitely fabricated through a self-assembly process on the water/air interface with subsequent in situ asymmetric modification at the oil/water interface. The interfacial asymmetric decoration strategy thus provides a novel pathway for achieving a 2D Janus hybrid film with asymmetric wettability and functionality.

scholarly journals Concentration Effects on the Dynamics of Liquid Crystalline Self-Assembly: Time-Resolved X-ray Scattering Studies

2011 ◽  
Vol 115 (11) ◽  
pp. 2176-2183 ◽  
Author(s):  
Marcel Petri ◽  
Andreas Menzel ◽  
Oliver Bunk ◽  
Gerhard Busse ◽  
Simone Techert
Keyword(s):  
Self Assembly ◽  
Liquid Crystalline ◽  
Concentration Effects ◽  
Time Resolved ◽  
X Ray ◽  
Assembly Time ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals SAXS/WAXS Investigation of Amyloid-β(16-22) Peptide Nanotubes

2021 ◽  
Vol 9 ◽  
Author(s):  
Theyencheri Narayanan ◽  
Axel Rüter ◽  
Ulf Olsson
Keyword(s):  
Self Assembly ◽  
Amyloid Β ◽  
Structural Elucidation ◽  
The Self ◽  
Assembly Process ◽  
Peptide Nanotubes ◽  
Short Peptide ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

This brief report presents an X-ray scattering investigation of self-assembled nanotubes formed by a short peptide. X-ray scattering methods enable multiscale structural elucidation of these nanotubes in solution under the same conditions involved in the self-assembly process. In particular, the dimensions of nanotubes and the crystalline organization within their walls can be determined quantitatively. This is illustrated in the case of amyloid-β(16-22) peptide nanotubes.

Dynamic Self-Assembly Process of a Designed Peptide

2013 ◽  
Vol 750-752 ◽  
pp. 1630-1634
Author(s):  
Li Ping Ruan ◽  
Zhi Hua Xing
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
The Self ◽  
Layer By Layer ◽  
Assembly Process ◽  
Force Microscopy ◽  
Atomic Force ◽  
Sheet Structure ◽  
Β Sheet ◽  
Layer Assembly

In this paper, we reported the dynamic self-assembly process of an half-sequence ionic self-complementarity peptide CH3CO-Pro-Ser-Phe-Cys-Phe-Lys-Phe-Glu-Pro-NH2, which could self-assemble into stable nanofibers and formed hydrogel consisting of >99% water. The dynamic self-assembly process was detected by circular dichroism (CD) and atomic force microscopy (AFM). CD spectrum revealed that the mainly contents of the peptide were regular β-sheet structure. The data indicated that though the secondary structure of the peptide formed immediately, the microstructure of the self-assembly process of the designed peptide formed slowly. AFM image illustrated that the self-assembly process was layer-by-layer assembly.

Small-angle X-ray scattering structural study of the nanofiber self-assembly process in supramolecular gels based on glucopyranosides

2014 ◽  
Vol 47 (4) ◽  
pp. 1284-1297 ◽  
Author(s):  
Marlon F. Abreu ◽  
Denise R. dos Santos ◽  
Carlos E. N. Gatts ◽  
Rosana Giacomini ◽  
Sergio L. Cardoso ◽  
...  
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Alkyl Chain ◽  
Hydroxyl Group ◽  
Assembly Process ◽  
Scanning Calorimetry ◽  
Oh Groups ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

This paper reports a study of the supramolecular self-assembly process of low molecular mass organic gelators in the formation of nanofiber networks. Methyl 4,6-O-benzylidene-α-D-glucopyranoside derivative compounds were designed to investigate the effect of substituents on the molecules' self-assembly properties. Gelators were prepared using two different substituent groups at position 4 of the aromatic ring: an electron-donating series (with n-alkoxyl groups) and an electron-withdrawing series (with n-alkoxycarbonyl groups), where n = 2, 3, 4, 8 and 16 C atoms. The gelation process in several gelator concentrations was studied in polar and apolar organic solvents. Differential scanning calorimetry revealed that the gelation temperature increases with the molar concentration and decreases with alkyl chain size in both series of gelators. Scanning electron microscopy images of the xerogel showed cylindrical aggregates. In situ small-angle X-ray scattering analysis corroborated a model of self-assembly based on one-dimensional nanofiber growth in a two-phase gel system, while X-ray powder diffraction revealed partial crystallization for the gelator compounds and for some gel samples. The infrared analyses of gels indicated that molecules undergo a self-assembly process via hydrogen bonding, suggesting that both OH groups are involved for samples of the n-alkoxycarbonyl series. On the other hand, the n-alkoxyl series aggregation process depends on the size of the alkyl chain. The compound with the smallest group, n-propoxyl, also undergoes self-assembly using both OH groups. Conversely, the rest of the n-alkoxyl series uses only one hydroxyl group.

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