The fractal self-assembly of the silk protein sericin

Soft Matter ◽  
2010 ◽  
Vol 6 (9) ◽  
pp. 2066 ◽  
Author(s):  
Tejas S. Khire ◽  
Joydip Kundu ◽  
Subhas C. Kundu ◽  
Vamsi K. Yadavalli
Keyword(s):  
Self Assembly ◽  
Silk Protein

scholarly journals A directed self-assembly quasi-spider silk protein expressed in Pichia pastoris

2017 ◽  
Vol 32 (2) ◽  
pp. 451-461 ◽  
Author(s):  
Bin Liu ◽  
Tao Wang ◽  
Liyan Xiao ◽  
Guilan Zhang ◽  
Guangshen Li ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Self Assembly ◽  
Spider Silk ◽  
Silk Protein ◽  
Spider Silk Protein

Self-assembly mechanisms of silk protein nanostructures on two-dimensional surfaces

Soft Matter ◽  
2012 ◽  
Vol 8 (18) ◽  
pp. 4952 ◽  
Author(s):  
Nicholas E. Kurland ◽  
Joydip Kundu ◽  
Shilpa Pal ◽  
Subhas C. Kundu ◽  
Vamsi K. Yadavalli
Keyword(s):  
Self Assembly ◽  
Silk Protein ◽  
Two Dimensional

scholarly journals Investigate the Effect of Thawing Process on the Self-Assembly of Silk Protein for Tissue Applications

2017 ◽  
Vol 2017 ◽  
pp. 1-16 ◽  
Author(s):  
Hiep Thi Nguyen ◽  
Hien Thu Luong ◽  
Hai Dai Nguyen ◽  
Hien Anh Tran ◽  
Khon Chan Huynh ◽  
...  
Keyword(s):  
Silk Fibroin ◽  
Self Assembly ◽  
Porous Scaffold ◽  
Building Blocks ◽  
Silk Protein ◽  
The Self ◽  
Porous Scaffolds ◽  
Protein Chain ◽  
Assembly Method ◽  
Thawing Process

Biological self-assembly is a process in which building blocks autonomously organize to form stable supermolecules of higher order and complexity through domination of weak, noncovalent interactions. For silk protein, the effect of high incubating temperature on the induction of secondary structure and self-assembly was well investigated. However, the effect of freezing and thawing on silk solution has not been studied. The present work aimed to investigate a new all-aqueous process to form 3D porous silk fibroin matrices using a freezing-assisted self-assembly method. This study proposes an experimental investigation and optimization of environmental parameters for the self-assembly process such as freezing temperature, thawing process, and concentration of silk solution. The optical images demonstrated the possibility and potential of −80ST48 treatment to initialize the self-assembly of silk fibroin as well as controllably fabricate a porous scaffold. Moreover, the micrograph images illustrate the assembly of silk protein chain in 7 days under the treatment of −80ST48 process. The surface morphology characterization proved that this method could control the pore size of porous scaffolds by control of the concentration of silk solution. The animal test showed the support of silk scaffold for cell adhesion and proliferation, as well as the cell migration process in the 3D implantable scaffold.

scholarly journals Nanoparticle self-assembly by a highly stable recombinant spider wrapping silk protein subunit

FEBS Letters ◽  
2013 ◽  
Vol 587 (19) ◽  
pp. 3273-3280 ◽  
Author(s):  
Lingling Xu ◽  
Marie-Laurence Tremblay ◽  
Kathleen E. Orrell ◽  
Jérémie Leclerc ◽  
Qing Meng ◽  
...  
Keyword(s):  
Self Assembly ◽  
Silk Protein ◽  
Protein Subunit

Self-Assembly from Low Dimension to Higher Conformation of GGX Motif in Spider Silk Protein

2009 ◽  
Vol 5 (4) ◽  
pp. 457-464 ◽  
Author(s):  
Qinghan Zhou ◽  
Juan Lin ◽  
Feng Yuan ◽  
Zhaoyang Ye ◽  
Feng Qiu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Silk Protein ◽  
Low Dimension ◽  
Spider Silk Protein

In vitro and in vivo polysaccharides assembly: ultrastructural and cytochemical study of growing plant cell wall components.

1978 ◽  
Vol 36 (2) ◽  
pp. 434-435
Author(s):  
D. Reis ◽  
B. Vian ◽  
J. C. Roland
Keyword(s):  
Cell Wall ◽  
Self Assembly ◽  
Plant Cell Wall ◽  
Higher Plants ◽  
Three Dimensional ◽  
Cytochemical Study ◽  
Wall Components

Wall morphogenesis in higher plants is a problem still open to controversy. Until now the possibility of a transmembrane control and the involvement of microtubules were mostly envisaged. Self-assembly processes have been observed in the case of walls of Chlamydomonas and bacteria. Spontaneous gelling interactions between xanthan and galactomannan from Ceratonia have been analyzed very recently. The present work provides indications that some processes of spontaneous aggregation could occur in higher plants during the formation and expansion of cell wall.Observations were performed on hypocotyl of mung bean (Phaseolus aureus) for which growth characteristics and wall composition have been previously defined.In situ, the walls of actively growing cells (primary walls) show an ordered three-dimensional organization (fig. 1). The wall is typically polylamellate with multifibrillar layers alternately transverse and longitudinal. Between these layers intermediate strata exist in which the orientation of microfibrils progressively rotates. Thus a progressive change in the morphogenetic activity occurs.

The Nature of Rapidly Extracted Phycocyanin from the Blue-Green Alga Plectonema Boryanum

1971 ◽  
Vol 29 ◽  
pp. 366-367
Author(s):  
M. Kessel ◽  
R. MacColl
Keyword(s):  
Self Assembly ◽  
Analytical Ultracentrifugation ◽  
Uranyl Acetate ◽  
The Self ◽  
Major Protein ◽  
Subunit Structure ◽  
Blue Green Alga ◽  
Thin Sections ◽  
Blue Green Algae ◽  
Cacodylate Buffer

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.

Video real-time imaging of artificial membranes during freeze-drying by cryo-electron microscopy

1988 ◽  
Vol 46 ◽  
pp. 16-17
Author(s):  
Alan S. Rudolph ◽  
Ronald R. Price
Keyword(s):  
Real Time ◽  
Self Assembly ◽  
Freeze Drying ◽  
Video Capture ◽  
Drying Process ◽  
Artificial Membranes ◽  
The Past ◽  
Cryo Electron Microscopy ◽  
Spherical Structures ◽  
Capture Techniques

We have employed cryoelectron microscopy to visualize events that occur during the freeze-drying of artificial membranes by employing real time video capture techniques. Artificial membranes or liposomes which are spherical structures within internal aqueous space are stabilized by water which provides the driving force for spontaneous self-assembly of these structures. Previous assays of damage to these structures which are induced by freeze drying reveal that the two principal deleterious events that occur are 1) fusion of liposomes and 2) leakage of contents trapped within the liposome [1]. In the past the only way to access these events was to examine the liposomes following the dehydration event. This technique allows the event to be monitored in real time as the liposomes destabilize and as water is sublimed at cryo temperatures in the vacuum of the microscope. The method by which liposomes are compromised by freeze-drying are largely unknown. This technique has shown that cryo-protectants such as glycerol and carbohydrates are able to maintain liposomal structure throughout the drying process.

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