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 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 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 Interfacial Crystallization and Supramolecular Self-Assembly of Spider Silk Inspired Protein at the Water-Air Interface

Materials ◽  
2021 ◽  
Vol 14 (15) ◽  
pp. 4239
Author(s):  
Pezhman Mohammadi ◽  
Fabian Zemke ◽  
Wolfgang Wagermaier ◽  
Markus B. Linder
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Assembly Process ◽  
Protein Solution ◽  
Time Resolved ◽  
Macromolecular Assembly ◽  
X Ray Scattering ◽  
Air Interface ◽  
Fundamental Research ◽  
Β Sheet

Macromolecular assembly into complex morphologies and architectural shapes is an area of fundamental research and technological innovation. In this work, we investigate the self-assembly process of recombinantly produced protein inspired by spider silk (spidroin). To elucidate the first steps of the assembly process, we examined highly concentrated and viscous pendant droplets of this protein in air. We show how the protein self-assembles and crystallizes at the water–air interface into a relatively thick and highly elastic skin. Using time-resolved in situ synchrotron X-ray scattering measurements during the drying process, we showed that the skin evolved to contain a high β-sheet amount over time. We also found that β-sheet formation strongly depended on protein concentration and relative humidity. These had a strong influence not only on the amount, but also on the ordering of these structures during the β-sheet formation process. We also showed how the skin around pendant droplets can serve as a reservoir for attaining liquid–liquid phase separation and coacervation from the dilute protein solution. Essentially, this study shows a new assembly route which could be optimized for the synthesis of new materials from a dilute protein solution and determine the properties of the final products.

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