Molecular complementarity and structural heterogeneity within co-assembled peptide β-sheet nanofibers

Nanoscale ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 4506-4518 ◽  
Author(s):  
Kong M. Wong ◽  
Yiming Wang ◽  
Dillon T. Seroski ◽  
Grant E. Larkin ◽  
Anil K. Mehta ◽  
...  
Keyword(s):  
Structural Heterogeneity ◽  
Self Assembling ◽  
Single Structure ◽  
Molecular Complementarity ◽  
Β Sheet

Charge-complementary peptides organize into co-assembled β-sheet nanofibers composed of multiple substructures rather than a single structure as seen in self-assembling peptides.

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.

Interaction of Self-Assembling β-Sheet Peptides with Phospholipid Monolayers: The Role of Aggregation State, Polarity, Charge and Applied Field

Langmuir ◽  
2009 ◽  
Vol 25 (5) ◽  
pp. 3289-3296 ◽  
Author(s):  
Elisabeth Protopapa ◽  
Steven Maude ◽  
Amalia Aggeli ◽  
Andrew Nelson
Keyword(s):  
Applied Field ◽  
Aggregation State ◽  
Self Assembling ◽  
Phospholipid Monolayers ◽  
Β Sheet

Self-assembling β-Sheet Tape Forming Peptides

2006 ◽  
Vol 18 (5) ◽  
pp. 435-443 ◽  
Author(s):  
R.P.W. Davies ◽  
A. Aggeli ◽  
A.J. Beevers ◽  
N. Boden ◽  
L.M. Carrick ◽  
...  
Keyword(s):  
Self Assembling ◽  
Β Sheet

Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity

2012 ◽  
Vol 51 (50) ◽  
pp. 12621-12625 ◽  
Author(s):  
Vanessa K. Morris ◽  
Rasmus Linser ◽  
Karyn L. Wilde ◽  
Anthony P. Duff ◽  
Margaret Sunde ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Structural Heterogeneity ◽  
Functional Amyloid ◽  
Solid State Nmr Spectroscopy ◽  
Β Sheet

Supramolecular β-Sheet and Nanofibril Formation by Self-assembling Tripeptides Containing an N-terminally Located γ-Aminobutyric acid Residue

2006 ◽  
Vol 18 (5) ◽  
pp. 455-464 ◽  
Author(s):  
Sudipta Ray ◽  
Michael G. B. Drew ◽  
Apurba Kumar Das ◽  
Arindam Banerjee
Keyword(s):  
Aminobutyric Acid ◽  
Self Assembling ◽  
Β Sheet

scholarly journals Design of Peptide-Based Supermolecules Using Self-Assembling β-Sheet Peptides

2010 ◽  
Vol 67 (10) ◽  
pp. 596-604
Author(s):  
Yoshiaki HIRANO ◽  
Shingou TAMIYA ◽  
Masahito OKA
Keyword(s):  
Self Assembling ◽  
Β Sheet

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 Modeling the Three-Dimensional Bioprinting Process of β-Sheet Self-Assembling Peptide Hydrogel Scaffolds

2020 ◽  
Vol 2 ◽  
Author(s):  
Irene Chiesa ◽  
Cosimo Ligorio ◽  
Amedeo F. Bonatti ◽  
Aurora De Acutis ◽  
Andrew M. Smith ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Hydrogel Scaffolds ◽  
Self Assembling ◽  
Β Sheet ◽  
Peptide Hydrogel

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.

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