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.

Self-assembly and gelation properties of α-helix versus β-sheet forming peptides

Soft Matter ◽  
2009 ◽  
Vol 5 (1) ◽  
pp. 193-202 ◽  
Author(s):  
A. Saiani ◽  
A. Mohammed ◽  
H. Frielinghaus ◽  
R. Collins ◽  
N. Hodson ◽  
...  
Keyword(s):  
Self Assembly ◽  
Sheet Forming ◽  
Α Helix ◽  
Β Sheet

Self-assembly of β-sheet forming peptides into chiral fibrillar aggregates

2007 ◽  
Vol 126 (24) ◽  
pp. 245104 ◽  
Author(s):  
Giovanni Bellesia ◽  
Joan-Emma Shea
Keyword(s):  
Self Assembly ◽  
Sheet Forming ◽  
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.

scholarly journals Extensive cellular uptake into endothelial cells of an amphipathic β-sheet forming peptide

FEBS Letters ◽  
1997 ◽  
Vol 415 (2) ◽  
pp. 196-199 ◽  
Author(s):  
Johannes Oehlke ◽  
Eberhard Krause ◽  
Burkhard Wiesner ◽  
Michael Beyermann ◽  
Michael Bienert
Keyword(s):  
Endothelial Cells ◽  
Cellular Uptake ◽  
Sheet Forming ◽  
Β Sheet

Self-Assembly of Nanofiber with Uniform Width from Wheel-Type Trigonal-β-Sheet-Forming Peptide

2008 ◽  
Vol 9 (3) ◽  
pp. 913-918 ◽  
Author(s):  
Kazuya Murasato ◽  
Kazunori Matsuura ◽  
Nobuo Kimizuka
Keyword(s):  
Self Assembly ◽  
Sheet Forming ◽  
Β Sheet

pH and salt controlled self-assembly of [1]benzothieno[3,2-b][1]-benzothiophene-peptide conjugates in supramolecular hydrogels

2021 ◽  
Author(s):  
Anna Fortunato ◽  
Alessandro Sanzone ◽  
Sara Mattiello ◽  
Luca Beverina ◽  
Miriam Mba
Keyword(s):  
Self Assembly ◽  
Sheet Forming ◽  
Structural Motif ◽  
Its Sequence ◽  
Peptide Conjugates ◽  
Β Sheet

We report here a [1]benzothieno[3,2-b][1]-benzothiophene (BTBT) derivative functionalized with a β-sheet forming peptide which alternates in its sequence Phe and Glu residues. The BTBT core is a popular structural motif...

scholarly journals Modification of β-Sheet Forming Peptide Hydrophobic Face: Effect on Self-Assembly and Gelation

Langmuir ◽  
2016 ◽  
Vol 32 (19) ◽  
pp. 4917-4923 ◽  
Author(s):  
Mohamed A. Elsawy ◽  
Andrew M. Smith ◽  
Nigel Hodson ◽  
Adam Squires ◽  
Aline F. Miller ◽  
...  
Keyword(s):  
Self Assembly ◽  
Sheet Forming ◽  
Β Sheet

scholarly journals Tandem-Homodimer of a β-Sheet-Forming Short Peptide Inhibits Random-to-β Structural Transition of Its Original Monomer

Processes ◽  
2020 ◽  
Vol 8 (11) ◽  
pp. 1421
Author(s):  
Kin-ya Tomizaki ◽  
Tomomi Iori ◽  
Hideyasu Fukushima ◽  
Yasuhiro Nakabayashi ◽  
Yoshiki Matsumoto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structural Transition ◽  
Amyloid Β ◽  
Sheet Forming ◽  
Aβ Peptide ◽  
Short Peptide ◽  
New Class ◽  
In Series ◽  
Chain Lengths ◽  
Β Sheet

There is an increasing interest in designing fibrillogenesis modulators for treating amyloid β (Aβ)-peptide-associated diseases. The use of Aβ fragment peptides and their derivatives, as well as nonpeptidyl natural products, is one promising approach to prevent Aβ fibrillation. In this study, we demonstrate that tandem-homodimers (TDs) of a β-sheet-forming short peptide in which the amino acid sequence is duplicated in series and joined via an amino alkanoic acid linker of different chain lengths, preventing the random-to-β structural transition of the original monomer. Ape5-TD, containing 5-amino pentanoate, most potently prevented this transition for at least five days by generating disordered aggregates with reduced tryptic stability. The linkers in the TDs generated this inhibitory activity, probably due to their bent conformations and hydrophobicity, appropriate for accommodating and twisting the monomers, resulting in irregular arrangements of the peptides. The present study could allow the design of a new class of protein/peptide fibrillogenesis modulators.

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