scholarly journals Tuning dynamic DNA- and peptide-driven self-assembly in DNA-peptide conjugates

2021 ◽  
Author(s):  
Emerald Taylor ◽  
Akiko Sato ◽  
Prashant Gudeangadi ◽  
David Beal ◽  
James Hopper ◽  
...  
Keyword(s):  
Self Assembly ◽  
Time Course ◽  
Chemical Diversity ◽  
The Self ◽  
Peptide Conjugates ◽  
Peptide Assembly ◽  
Aging Studies ◽  
Aging Study ◽  
High Level ◽  
Single Macromolecule

DNA-peptide conjugates offer an opportunity to marry the benefits of both biomolecules, such as the high level of control and programmability found with DNA and the chemical diversity and biological stability of peptides. These hybrid systems offer great potential in fields such as therapeutics, nanotechnology, and robotics to name a few. Using the first DNA-β-turn peptide conjugate, we present three studies designed to investigate the self-assembly of DNA-peptide conjugates over a period of 28 days. Time-course studies, such as these have not been previously conducted for DNA-peptide conjugates, although they are common in pure peptide assembly, for example in amyloid research. By using aging studies to assess the structures produced, we gain insights into the dynamic nature of these systems. The first study explores the influence varying amounts of DNA-peptide conjugates have on the self-assembly of our parent peptide. Study 2 explores how DNA and peptide can work together to change the structures observed during aging. Study 3 investigates the presence of orthogonality within our system by switching the DNA and peptide control on and off independently. These results show that two orthogonal self-assemblies can be combined and operated either independently or in tandem within a single macromolecule, with both spatial and temporal effects upon the resultant nanostructures.

scholarly journals Tuning dynamic DNA- and peptide-driven self-assembly in DNA-peptide conjugates

2021 ◽  
Author(s):  
Emerald Taylor ◽  
Akiko Sato ◽  
Prashant Gudeangadi ◽  
David Beal ◽  
James Hopper ◽  
...  
Keyword(s):  
Self Assembly ◽  
Time Course ◽  
Chemical Diversity ◽  
The Self ◽  
Peptide Conjugates ◽  
Peptide Assembly ◽  
Aging Studies ◽  
Aging Study ◽  
High Level ◽  
Single Macromolecule

DNA-peptide conjugates offer an opportunity to marry the benefits of both biomolecules, such as the high level of control and programmability found with DNA and the chemical diversity and biological stability of peptides. These hybrid systems offer great potential in fields such as therapeutics, nanotechnology, and robotics to name a few. Using the first DNA-β-turn peptide conjugate, we present three studies designed to investigate the self-assembly of DNA-peptide conjugates over a period of 28 days. Time-course studies, such as these have not been previously conducted for DNA-peptide conjugates, although they are common in pure peptide assembly, for example in amyloid research. By using aging studies to assess the structures produced, we gain insights into the dynamic nature of these systems. The first study explores the influence varying amounts of DNA-peptide conjugates have on the self-assembly of our parent peptide. Study 2 explores how DNA and peptide can work together to change the structures observed during aging. Study 3 investigates the presence of orthogonality within our system by switching the DNA and peptide control on and off independently. These results show that two orthogonal self-assemblies can be combined and operated either independently or in tandem within a single macromolecule, with both spatial and temporal effects upon the resultant nanostructures.

Folding induced supramolecular assembly into pH-responsive nanorods with a protein repellent shell

2018 ◽  
Vol 54 (4) ◽  
pp. 401-404 ◽  
Author(s):  
R. Otter ◽  
K. Klinker ◽  
D. Spitzer ◽  
M. Schinnerer ◽  
M. Barz ◽  
...  
Keyword(s):  
Self Assembly ◽  
Supramolecular Assembly ◽  
The Self ◽  
Core Shell ◽  
Ph Responsive ◽  
Peptide Conjugates ◽  
Β Sheets

ABA′ triblock peptide–polysarcosine–peptide conjugates fold into antiparallel β-sheets, which promotes the self-assembly into polysarcosine-shielded core–shell nanorods with protein repellent properties.

Doxorubicin-reinforced supramolecular hydrogels of RGD-derived peptide conjugates for pH-responsive drug delivery

2019 ◽  
Vol 17 (15) ◽  
pp. 3853-3860 ◽  
Author(s):  
Leixia Mei ◽  
Keming Xu ◽  
Ziran Zhai ◽  
Suyun He ◽  
Tingting Zhu ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Self Assembly ◽  
The Self ◽  
Ph Responsive ◽  
Peptide Conjugates

Doxorubicin reinforced the self-assembly of RGD-derived peptide conjugates responsive to mild acidity.

scholarly journals Morphological transformation enhances Tumor Retention by Regulating the Self-assembly of Doxorubicin-peptide Conjugates

Theranostics ◽  
2020 ◽  
Vol 10 (18) ◽  
pp. 8162-8178
Author(s):  
Liu Xu ◽  
Yutong Wang ◽  
Chenqi Zhu ◽  
Shujing Ren ◽  
Yurou Shao ◽  
...  
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Morphological Transformation ◽  
Peptide Conjugates ◽  
Tumor Retention

The crown ether size and stereochemistry affect the self-assembly, hydrogelation, and cellular interactions of crown ether/peptide conjugates

2020 ◽  
Vol 8 (43) ◽  
pp. 9961-9970
Author(s):  
Abdelreheem Abdelfatah Saddik ◽  
Mohiuddin Mohammed ◽  
Hsin-Chieh Lin
Keyword(s):  
Cell Adhesion ◽  
Crown Ether ◽  
Self Assembly ◽  
The Self ◽  
Ring Size ◽  
Cellular Interactions ◽  
Peptide Conjugates ◽  
Nanofiber Morphology ◽  
Cell Adhesion And Proliferation

Crown ether ring size affects nanofiber morphology of hydrogels upon conjugation with D- and L-phenylalanine dipeptides. Random nanofibers showed enhanced cell adhesion and proliferation whereas twisted nanofibers displayed weak cell attachments.

scholarly journals Fine structural tuning of the assembly of ECM peptide conjugates via slight sequence modifications

2020 ◽  
Vol 6 (41) ◽  
pp. eabd3033
Author(s):  
Jingya Qin ◽  
Jennifer D. Sloppy ◽  
Kristi L. Kiick
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Morphological Transition ◽  
Biological Applications ◽  
Peptide Conjugates ◽  
Collagen Binding ◽  
Drug Delivery Vehicles ◽  
Delivery Vehicles ◽  
Lower Transition ◽  
The Impact

The self-assembly of nanostructures from conjugates of elastin-like peptides and collagen-like peptides (ELP-CLP) has been studied as means to produce thermoresponsive, collagen-binding drug delivery vehicles. Motivated by our previous work in which ELP-CLP conjugates successfully self-assembled into vesicles and platelet-like nanostructures, here, we extend our library of ELP-CLP bioconjugates to a series of tryptophan/phenylalanine-containing ELPs and GPO-based CLPs [W2Fx-b-(GPO)y] with various domain lengths to determine the impact of these modifications on the thermoresponsiveness and morphology. The lower transition temperature of the conjugates with longer ELP or CLP domains enables the formation of well-defined nanoparticles near physiological temperature. Moreover, the morphological transition from vesicles to platelet-like nanostructures occurred when the ratio of the lengths of ELP/CLP decreased. Given the previously demonstrated ability of many ELP-CLP bioconjugates to bind to both hydrophobic drugs and collagen-containing materials, our results suggest new opportunities for designing specific thermoresponsive nanostructures for targeted biological applications.

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.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

Nanoscale Self-Assembly Using Ion and Electron Beam Techniques: A Rapid Review

MRS Advances ◽  
2020 ◽  
Vol 5 (64) ◽  
pp. 3507-3520
Author(s):  
Chunhui Dai ◽  
Kriti Agarwal ◽  
Jeong-Hyun Cho
Keyword(s):  
Electron Beam ◽  
Self Assembly ◽  
Ion Beam ◽  
Three Dimensional ◽  
The Self ◽  
Stress Generation ◽  
Rapid Review ◽  
High Yield ◽  
3D Nanostructures ◽  
Self Assembled

AbstractNanoscale self-assembly, as a technique to transform two-dimensional (2D) planar patterns into three-dimensional (3D) nanoscale architectures, has achieved tremendous success in the past decade. However, an assembly process at nanoscale is easily affected by small unavoidable variations in sample conditions and reaction environment, resulting in a low yield. Recently, in-situ monitored self-assembly based on ion and electron irradiation has stood out as a promising candidate to overcome this limitation. The usage of ion and electron beam allows stress generation and real-time observation simultaneously, which significantly enhances the controllability of self-assembly. This enables the realization of various complex 3D nanostructures with a high yield. The additional dimension of the self-assembled 3D nanostructures opens the possibility to explore novel properties that cannot be demonstrated in 2D planar patterns. Here, we present a rapid review on the recent achievements and challenges in nanoscale self-assembly using electron and ion beam techniques, followed by a discussion of the novel optical properties achieved in the self-assembled 3D nanostructures.

Folding-Controlled Assembly of Ortho-Phenylene-Based Macrocycles

2020 ◽  
Author(s):  
Viraj kirinda ◽  
Scott Hartley
Keyword(s):  
Self Assembly ◽  
Structural Control ◽  
Structural Changes ◽  
Condensation Product ◽  
Gel Permeation Chromatography ◽  
Emergent Behavior ◽  
Order Structure ◽  
High Level ◽  
Alkoxy Groups ◽  
Energy Surfaces

The self-assembly of foldamers into macrocycles is a simple approach to non-biological higher-order structure. Previous work on the co-assembly of ortho-phenylene foldamers with rod-shaped linkers has shown that folding and self-assembly affect each other; that is, the combination leads to new emergent behavior, such as access to otherwise unfavorable folding states. To this point this relationship has been passive. Here, we demonstrate control of self-assembly by manipulating the foldamers’ conformational energy surfaces. A series of o-phenylene decamers and octamers have been assembled into macrocycles using imine condensation. Product distributions were analyzed by gel-permeation chromatography and molecular geometries extracted from a combination of NMR spectroscopy and computational chemistry. The assembly of o-phenylene decamers functionalized with alkoxy groups or hydrogens gives both [2+2] and [3+3] macrocycles. The mixture results from a subtle balance of entropic and enthalpic effects in these systems: the smaller [2+2] macrocycles are entropically favored but require the oligomer to misfold, whereas a perfectly folded decamer fits well within the larger [3+3] macrocycle that is entropically disfavored. Changing the substituents to fluoro groups, however, shifts assembly quantitatively to the [3+3] macrocycle products, even though the structural changes are well-removed from the functional groups directly participating in bond formation. The electron-withdrawing groups favor folding in these systems by strengthening arene–arene stacking interactions, increasing the enthalpic penalty to misfolding. The architectural changes are substantial even though the chemical perturbation is small: analogous o-phenylene octamers do not fit within macrocycles when perfectly folded, and quantitatively misfold to give small macrocycles regardless of substitution. Taken together, these results represent both a high level of structural control in structurally complex foldamer systems and the demonstration of large-amplitude structural changes as a consequence of a small structural effects.

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