Self-assembled β-Sheet Peptide Nanofibers for Efficient Antigen Delivery

2013 ◽  
Vol 42 (11) ◽  
pp. 1441-1443 ◽  
Author(s):  
Tomonori Waku ◽  
Yuichi Kitagawa ◽  
Kazufumi Kawabata ◽  
Saki Nishigaki ◽  
Shigeru Kunugi ◽  
...  
Keyword(s):  
Antigen Delivery ◽  
Peptide Nanofibers ◽  
Self Assembled ◽  
Β Sheet

scholarly journals Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes

2020 ◽  
Vol 21 (24) ◽  
pp. 9518
Author(s):  
Tomonori Waku ◽  
Ayane Kasai ◽  
Akio Kobori ◽  
Naoki Tanaka
Keyword(s):  
Chain Length ◽  
Surface Pressure ◽  
Cell Membranes ◽  
Langmuir Monolayers ◽  
Antigenic Peptides ◽  
Design Guideline ◽  
Peptide Nanofibers ◽  
Model Cell ◽  
Self Assembled ◽  
Β Sheet

Self-assembled peptide nanofibers (NFs) obtained from β-sheet peptides conjugated with drugs, including antigenic peptides, have recently attracted significant attention. However, extensive studies on the interactions of β-sheet peptide NFs with model cell membranes have not been reported. In this study, we investigated the interactions between three types of NFs, composed of PEG-peptide conjugates with different ethylene glycol (EG) lengths (6-, 12- and 24-mer), and dipalmitoylphosphatidylcholine (DPPC) Langmuir membranes. When increasing the EG chain length, those interactions significantly decreased considering measurements in the presence of the NFs of: (i) changes in surface pressure of the DPPC Langmuir monolayers and (ii) surface pressure–area (π–A) compression isotherms of DPPC. Because the observed trend was similar to the EG length dependency with regard to cellular association and cytotoxicity of the NFs that was reported previously, the interaction of NFs with phospholipid membranes represented a crucial factor to determine the cellular association and toxicity of the NFs. In contrast to NFs, no changes were observed with varying EG chain length on the interaction of the building block peptide with the DPPC membrane. The results obtained herein can provide a design guideline on the formulation of β-sheet peptide NFs, which may broaden its potential.

Self-assembled IKVAV peptide nanofibers promote adherence of PC12 cells

2006 ◽  
Vol 26 (5) ◽  
pp. 594-596 ◽  
Author(s):  
Yongchao Wu ◽  
Qixin Zheng ◽  
Jingyuan Du ◽  
Yulin Song ◽  
Bin Wu ◽  
...  
Keyword(s):  
Pc12 Cells ◽  
Peptide Nanofibers ◽  
Self Assembled

Tuning carbohydrate density enhances protein binding and inhibition by glycosylated β-sheet peptide nanofibers

2018 ◽  
Vol 6 (9) ◽  
pp. 2327-2335 ◽  
Author(s):  
Antonietta Restuccia ◽  
Gregory A. Hudalla
Keyword(s):  
Protein Binding ◽  
Binding Affinity ◽  
Binding Proteins ◽  
Carbohydrate Binding ◽  
Peptide Nanofibers ◽  
Carbohydrate Binding Proteins ◽  
Β Sheet

The efficacy of glycosylated β-sheet peptide nanofibers for inhibiting carbohydrate-binding proteins can be increased by tuning carbohydrate density to maximize protein binding affinity.

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

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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