The fabrication of self-assembling peptides into nanofiber scaffolds through molecular self-assembly

2004 ◽  
Vol 823 ◽  
Author(s):  
Xiaojun Zhao ◽  
Jessica Dai ◽  
Shuguang Zhang
Keyword(s):  
Cell Cultures ◽  
Self Assembly ◽  
Rational Design ◽  
Biophysical Properties ◽  
Ph Values ◽  
Nanofiber Scaffold ◽  
Self Assembling ◽  
Nanofiber Scaffolds ◽  
D Cell ◽  
Β Sheet

AbstractWe designed and fabricated a class of self-assembling peptides into nanofiber scaffolds. KLDL-12 has been shown to be a permissible nanofiber scaffold for chondrocytes in cartilage 3-D cell cultures. However, the biochemical, structural, and biophysical properties of KLDL-12 remain unclear. We show that KLDL-12 peptides form stable β-sheet structures at different pH values and that KLDL-12 and RIDI-12 self-assemble into nanofibers. The nanofiber length, though, is sensitive to pH changes. These results not only suggest the importance of electrostatic attraction or repulsion affecting the fiber lengths but also provide us with useful information for rational design and fabrication of peptide scaffolds.

The fabrication of self-assembling peptides into nanofiber scaffolds through molecular self-assembly

2004 ◽  
Vol 820 ◽  
Author(s):  
Xiaojun Zhao ◽  
Jessica Dai ◽  
Shuguang Zhang
Keyword(s):  
Cell Cultures ◽  
Self Assembly ◽  
Rational Design ◽  
Biophysical Properties ◽  
Ph Values ◽  
Nanofiber Scaffold ◽  
Self Assembling ◽  
Nanofiber Scaffolds ◽  
D Cell ◽  
Β Sheet

AbstractWe designed and fabricated a class of self-assembling peptides into nanofiber scaffolds. KLDL-12 has been shown to be a permissible nanofiber scaffold for chondrocytes in cartilage 3-D cell cultures. However, the biochemical, structural, and biophysical properties of KLDL- 12 remain unclear. We show that KLDL-12 peptides form stable β-sheet structures at different pH values and that KLDL-12 and RIDI-12 self-assemble into nanofibers. The nanofiber length, though, is sensitive to pH changes. These results not only suggest the importance of electrostatic attraction or repulsion affecting the fiber lengths but also provide us with useful information for rational design and fabrication of peptide scaffolds.

scholarly journals Dual self-assembly of supramolecular peptide nanotubes to provide stabilisation in water

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Julia Y. Rho ◽  
Henry Cox ◽  
Edward D. H. Mansfield ◽  
Sean H. Ellacott ◽  
Raoul Peltier ◽  
...  
Keyword(s):  
Self Assembly ◽  
Supramolecular Assembly ◽  
Ordered Structures ◽  
Peptide Bonds ◽  
Self Assembling ◽  
Peptide Hydrogen ◽  
Aqueous Conditions ◽  
Β Sheet ◽  
Peptide Core ◽  
Hydrogen Bonded

Abstract Self-assembling peptides have the ability to spontaneously aggregate into large ordered structures. The reversibility of the peptide hydrogen bonded supramolecular assembly make them tunable to a host of different applications, although it leaves them highly dynamic and prone to disassembly at the low concentration needed for biological applications. Here we demonstrate that a secondary hydrophobic interaction, near the peptide core, can stabilise the highly dynamic peptide bonds, without losing the vital solubility of the systems in aqueous conditions. This hierarchical self-assembly process can be used to stabilise a range of different β-sheet hydrogen bonded architectures.

Designer D-form self-assembling peptide nanofiber scaffolds for 3-dimensional cell cultures

Biomaterials ◽  
2013 ◽  
Vol 34 (21) ◽  
pp. 4902-4913 ◽  
Author(s):  
Zhongli Luo ◽  
Yuanyuan Yue ◽  
Yanfang Zhang ◽  
Xiao Yuan ◽  
Jianping Gong ◽  
...  
Keyword(s):  
Cell Cultures ◽  
3 Dimensional ◽  
Self Assembling ◽  
Nanofiber Scaffolds ◽  
Dimensional Cell

Designer self-assembling peptide nanofiber scaffolds for 3D tissue cell cultures

2005 ◽  
Vol 15 (5) ◽  
pp. 413-420 ◽  
Author(s):  
Shuguang Zhang ◽  
Fabrizio Gelain ◽  
Xiaojun Zhao
Keyword(s):  
Cell Cultures ◽  
Tissue Cell ◽  
Self Assembling ◽  
Nanofiber Scaffolds

scholarly journals A Universal Chemical Method for Rational Design of Protein-based Nanoreactors

2021 ◽  
Author(s):  
Mullapudi Mohan Reddy ◽  
Punita Bathla ◽  
Britto S. Sandanaraj
Keyword(s):  
Self Assembly ◽  
Rational Design ◽  
Chemical Method ◽  
Living Cells ◽  
Protein Labeling ◽  
Self Assembling ◽  
Naturally Occurring ◽  
General Chemical ◽  
Chemical Strategy ◽  
Artificial Protein

AbstractSelf-assembly of a monomeric protease to form a multi-subunit protein complex “proteasome” enables targeted protein degradation in living cells. The naturally occurring proteasomes serve as an inspiration and blueprint for the design of artificial protein-based nanoreactors. Here we disclose a general chemical strategy for the design of proteasome-like nanoreactors. Micelle-assisted protein labeling (MAPLab) technology along with the N-terminal bioconjugation strategy is utilized for the synthesis of a well-defined monodisperse self-assembling semi-synthetic protease. The designer protein is programmed to self-assemble into a proteasome-like nanostructure which preserves the functional properties of native protease.

scholarly journals Control over the fibrillization yield by varying the oligomeric nucleation propensities of self-assembling peptides

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Chun Yin Jerry Lau ◽  
Federico Fontana ◽  
Laurens D. B. Mandemaker ◽  
Dennie Wezendonk ◽  
Benjamin Vermeer ◽  
...  
Keyword(s):  
Thermodynamic Stability ◽  
Self Assembly ◽  
Biomedical Applications ◽  
Supramolecular Assemblies ◽  
Mechanistic Studies ◽  
Molecular Changes ◽  
Self Assembling ◽  
Charged Residues ◽  
Β Sheet

AbstractSelf-assembling peptides are an exemplary class of supramolecular biomaterials of broad biomedical utility. Mechanistic studies on the peptide self-assembly demonstrated the importance of the oligomeric intermediates towards the properties of the supramolecular biomaterials being formed. In this study, we demonstrate how the overall yield of the supramolecular assemblies are moderated through subtle molecular changes in the peptide monomers. This strategy is exemplified with a set of surfactant-like peptides (SLPs) with different β-sheet propensities and charged residues flanking the aggregation domains. By integrating different techniques, we show that these molecular changes can alter both the nucleation propensity of the oligomeric intermediates and the thermodynamic stability of the fibril structures. We demonstrate that the amount of assembled nanofibers are critically defined by the oligomeric nucleation propensities. Our findings offer guidance on designing self-assembling peptides for different biomedical applications, as well as insights into the role of protein gatekeeper sequences in preventing amyloidosis.

Designer functionalised self-assembling peptide nanofibre scaffolds for cartilage tissue engineering

2014 ◽  
Vol 16 ◽  
Author(s):  
Bin He ◽  
Xiao Yuan ◽  
Aiguo Zhou ◽  
Hua Zhang ◽  
Dianming Jiang
Keyword(s):  
Tissue Engineering ◽  
Self Assembly ◽  
Rational Design ◽  
Cartilage Tissue Engineering ◽  
Cartilage Tissue ◽  
Cartilage Defects ◽  
Regenerative Capacity ◽  
Self Assembling ◽  
Important Approach ◽  
Biomaterial Scaffolds

Owing to the limited regenerative capacity of cartilage tissue, cartilage repair remains a challenge in clinical treatment. Tissue engineering has emerged as a promising and important approach to repair cartilage defects. It is well known that material scaffolds are regarded as a fundamental element of tissue engineering. Novel biomaterial scaffolds formed by self-assembling peptides consist of nanofibre networks highly resembling natural extracellular matrices, and their fabrication is based on the principle of molecular self-assembly. Indeed, peptide nanofibre scaffolds have obtained much progress in repairing various damaged tissues (e.g. cartilage, bone, nerve, heart and blood vessel). This review outlines the rational design of peptide nanofibre scaffolds and their potential in cartilage tissue engineering.

Rational design of patchy colloidsvialandscape engineering

2018 ◽  
Vol 3 (1) ◽  
pp. 49-65 ◽  
Author(s):  
Andrew W. Long ◽  
Andrew L. Ferguson
Keyword(s):  
Free Energy ◽  
Self Assembly ◽  
Rational Design ◽  
Energy Landscape ◽  
Building Blocks ◽  
Inverse Design ◽  
Free Energy Landscape ◽  
New Approach ◽  
Self Assembling

A new approach for inverse design of self-assembling building blocks by rational sculpting of the underlying self-assembly free energy landscape.

scholarly journals Carbocycle-Based Organogelators: Influence of Chirality and Structural Features on Their Supramolecular Arrangements and Properties

Gels ◽  
2021 ◽  
Vol 7 (2) ◽  
pp. 54
Author(s):  
Rosa M. Ortuño
Keyword(s):  
Smart Materials ◽  
Self Assembly ◽  
Rational Design ◽  
Structural Features ◽  
Stimuli Responsive ◽  
Polycyclic Compounds ◽  
Relative Configuration ◽  
Responsive Materials ◽  
Self Assembling ◽  
Donor Acceptor

The rational design and engineer of organogel-based smart materials and stimuli-responsive materials with tuned properties requires the control of the non-covalent forces driving the hierarchical self-assembly. Chirality, as well as cis/trans relative configuration, also plays a crucial role promoting the morphology and characteristics of the aggregates. Cycloalkane derivatives can provide chiral chemical platforms allowing the incorporation of functional groups and hydrophobic structural units able for a convenient molecular stacking leading to gels. Restriction of the conformational freedom imposed by the ring strain is also a contributing issue that can be modulated by the inclusion of flexible segments. In addition, donor/acceptor moieties can also be incorporated favoring the interactions with light or with charged species. This review offers a perspective on the abilities and properties of carbocycle-based organogelators starting from simple cycloalkane derivatives, which were the key to establish the basis for an effective self-assembling, to sophisticated polycyclic compounds with manifold properties and applications.

scholarly journals Advancement of Peptide Nanobiotechnology via Emerging Microfluidic Technology

Micromachines ◽  
2019 ◽  
Vol 10 (10) ◽  
pp. 627 ◽  
Author(s):  
Chan ◽  
Tay
Keyword(s):  
Functional Groups ◽  
Cell Cultures ◽  
Self Assembly ◽  
Nanoparticle Size ◽  
Promising Technique ◽  
Self Assembling ◽  
Microfluidic Technology ◽  
Physical Shape ◽  
Peptide Nanoparticles ◽  
Shape And Size

Peptide nanotechnology has experienced a long and enduring development since its inception. Many different applications have been conceptualized, which depends on the functional groups present on the peptide and the physical shape/size of the peptide nanostructures. One of the most prominent nanostructures formed by peptides are nanoparticles. Until recently, however, it has been challenging to engineer peptide nanoparticles with low dispersity. An emerging and promising technique involves the utility of microfluidics to produce a solution of peptide nanoparticles with narrow dispersity. In this process, two or more streams of liquid are focused together to create conditions that are conducive towards the formation of narrowly dispersed samples of peptide nanoparticles. This makes it possible to harness peptide nanoparticles for the myriad of applications that are dependent on nanoparticle size and uniformity. In this focus review, we aim to show how microfluidics may be utilized to (1) study peptide self-assembly, which is critical to controlling nanostructure shape and size, and peptide-interface interactions, and (2) generate self-assembling peptide-based microgels for miniaturized cell cultures. These examples will illustrate how the emerging microfluidic approach promises to revolutionize the production and application of peptide nanoparticles in ever more diverse fields than before.

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