Artificial Peptide-Nanospheres Self-Assembled from Three-Way Junctions of β-Sheet-Forming Peptides

2005 ◽  
Vol 127 (29) ◽  
pp. 10148-10149 ◽  
Author(s):  
Kazunori Matsuura ◽  
Kazuya Murasato ◽  
Nobuo Kimizuka
Keyword(s):  
Sheet Forming ◽  
Self Assembled ◽  
Β Sheet

scholarly journals Molecular Design of β-Hairpin Peptides for Material Construction

MRS Bulletin ◽  
2008 ◽  
Vol 33 (5) ◽  
pp. 530-535 ◽  
Author(s):  
Ronak V. Rughani ◽  
Joel P. Schneider
Keyword(s):  
Material Properties ◽  
Molecular Design ◽  
Molecular Level ◽  
Sheet Forming ◽  
Environmental Stimulus ◽  
Sheet Structure ◽  
Amphiphilic Peptide ◽  
Self Assembled ◽  
Hairpin Peptides ◽  
Β Sheet

AbstractSelf-assembled materials composed of β-sheet forming peptides hold promise as therapeutics and novel biomaterials. This article focuses on the design and engineering of amphiphilic peptide sequences, especially β-hairpins. Peptides can be designed to intramolecularly fold and then self-assemble on cue, affording hydrogels rich in β-sheet structure. Hydrogels having distinct material properties can be designed at the molecular level by modulating either the peptide's sequence or the environmental stimulus used to trigger folding and assembly, leading to gelation.

The alkyl linkers in tandem-homodimers of a β-sheet-forming nonapeptide affect the self-assembled nanostructures

2016 ◽  
Vol 26 (11) ◽  
pp. 2659-2662 ◽  
Author(s):  
Kin-ya Tomizaki ◽  
Atsushi Tanaka ◽  
Hiroki Shimada ◽  
Koki Nishizawa ◽  
Tsubasa Wada ◽  
...  
Keyword(s):  
Sheet Forming ◽  
The Self ◽  
Self Assembled ◽  
Β Sheet

Spectroscopic Studies of Structural Changes in Two β-Sheet-Forming Peptides Show an Ensemble of Structures that Unfold Noncooperatively†

Biochemistry ◽  
2003 ◽  
Vol 42 (15) ◽  
pp. 4321-4332 ◽  
Author(s):  
Serguei V. Kuznetsov ◽  
Jovencio Hilario ◽  
Timothy A. Keiderling ◽  
Anjum Ansari
Keyword(s):  
Structural Changes ◽  
Spectroscopic Studies ◽  
Sheet Forming ◽  
Β Sheet

scholarly journals Effect of the Hydrophilic-Hydrophobic Balance of Antigen-Loaded Peptide Nanofibers on Their Cellular Uptake, Cellular Toxicity, and Immune Stimulatory Properties

2019 ◽  
Vol 20 (15) ◽  
pp. 3781 ◽  
Author(s):  
Tomonori Waku ◽  
Saki Nishigaki ◽  
Yuichi Kitagawa ◽  
Sayaka Koeda ◽  
Kazufumi Kawabata ◽  
...  
Keyword(s):  
Cellular Uptake ◽  
Self Assembly ◽  
Sheet Forming ◽  
Design Guidelines ◽  
Cellular Interactions ◽  
Antigenic Peptides ◽  
Peptide Nanofibers ◽  
Dc Line ◽  
Chain Lengths ◽  
Β Sheet

Recently, nanofibers (NFs) formed from antigenic peptides conjugated to β-sheet-forming peptides have attracted much attention as a new generation of vaccines. However, studies describing how the hydrophilic-hydrophobic balance of NF components affects cellular interactions of NFs are limited. In this report, three different NFs were prepared by self-assembly of β-sheet-forming peptides conjugated with model antigenic peptides (SIINFEKL) from ovalbumin and hydrophilic oligo-ethylene glycol (EG) of differing chain lengths (6-, 12- and 24-mer) to investigate the effect of EG length of antigen-loaded NFs on their cellular uptake, cytotoxicity, and dendritic cell (DC)-stimulation ability. We used an immortal DC line, termed JAWS II, derived from bone marrow-derived DCs of a C57BL/6 p53-knockout mouse. The uptake of NFs, consisting of the EG 12-mer by DCs, was the most effective and activated DC without exhibiting significant cytotoxicity. Increasing the EG chain length significantly reduced cellular entry and DC activation by NFs. Conversely, shortening the EG chain enhanced DC activation but increased toxicity and impaired water-dispersibility, resulting in low cellular uptake. These results show that the interaction of antigen-loaded NFs with cells can be tuned by the EG length, which provides useful design guidelines for the development of effective NF-based vaccines.

Laser-Induced Alignment of Self-Assembled Films of an Oligopeptide β Sheet on the Water Surface

2010 ◽  
Vol 122 (13) ◽  
pp. 2404-2407 ◽  
Author(s):  
Atalia Birman ◽  
Kristian Kjaer ◽  
Yehiam Prior ◽  
Iftach Nevo ◽  
Leslie Leiserowitz
Keyword(s):  
Water Surface ◽  
Self Assembled ◽  
Β Sheet

scholarly journals Tunable Pentapeptide Self-Assembled β-Sheet Hydrogels

2018 ◽  
Vol 130 (26) ◽  
pp. 7835-7839 ◽  
Author(s):  
David E. Clarke ◽  
Christopher D. J. Parmenter ◽  
Oren A. Scherman
Keyword(s):  
Self Assembled ◽  
Β Sheet

scholarly journals Tunable Pentapeptide Self-Assembled β-Sheet Hydrogels

2018 ◽  
Vol 57 (26) ◽  
pp. 7709-7713 ◽  
Author(s):  
David E. Clarke ◽  
Christopher D. J. Parmenter ◽  
Oren A. Scherman
Keyword(s):  
Self Assembled ◽  
Β Sheet

Nanotubular self-organization of amide dendrons with focal β-sheet forming peptide units

Soft Matter ◽  
2016 ◽  
Vol 12 (36) ◽  
pp. 7453-7456 ◽  
Author(s):  
Jeonghun Lee ◽  
Hyunil Jang ◽  
Jonghwan Park ◽  
Chulhee Kim
Keyword(s):  
Sheet Forming ◽  
Self Organization ◽  
Β Sheet

Amyloid-Derived Peptide Forms Self-Assembled Monolayers on Gold Nanoparticle with a Curvature-Dependent β-Sheet Structure

ACS Nano ◽  
2012 ◽  
Vol 6 (2) ◽  
pp. 1416-1426 ◽  
Author(s):  
Christopher P. Shaw ◽  
David A. Middleton ◽  
Martin Volk ◽  
Raphaël Lévy
Keyword(s):  
Gold Nanoparticle ◽  
Self Assembled Monolayers ◽  
Sheet Structure ◽  
Assembled Monolayers ◽  
Self Assembled ◽  
Β Sheet
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