Metallopolymer−Peptide Conjugates:  Synthesis and Self-Assembly of Polyferrocenylsilane Graft and Block Copolymers Containing a β-Sheet Forming Gly-Ala-Gly-Ala Tetrapeptide Segment

2006 ◽  
Vol 7 (4) ◽  
pp. 1005-1010 ◽  
Author(s):  
Guido W. M. Vandermeulen ◽  
Kyoung Taek Kim ◽  
Zhuo Wang ◽  
Ian Manners
Keyword(s):  
Block Copolymers ◽  
Self Assembly ◽  
Sheet Forming ◽  
Peptide Conjugates ◽  
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 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

Self-assembly of photochromic diarylethene–peptide conjugates stabilized by β-sheet formation at the liquid/graphite interface

2019 ◽  
Vol 55 (35) ◽  
pp. 5099-5102 ◽  
Author(s):  
Nobuhiko Nishitani ◽  
Takashi Hirose ◽  
Kenji Matsuda
Keyword(s):  
Self Assembly ◽  
Octanoic Acid ◽  
Scanning Tunnelling Microscopy ◽  
Two Dimensional ◽  
Peptide Conjugates ◽  
Strong Stabilization ◽  
Scanning Tunnelling ◽  
Tunnelling Microscopy ◽  
Stabilization Effect ◽  
Β Sheet

Two-dimensional (2-D) self-assembly of diarylethene (DAE)–peptide conjugates at the octanoic acid/graphite interface was investigated by scanning tunnelling microscopy (STM) and strong stabilization effect of β-sheet formation was revealed.

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

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

Self-Assembly of Hydrogels From Elastin-Mimetic Block Copolymers

2002 ◽  
Vol 724 ◽  
Author(s):  
Elizabeth R. Wright ◽  
R. Andrew McMillan ◽  
Alan Cooper ◽  
Robert P. Apkarian ◽  
Vincent P. Conticello
Keyword(s):  
Block Copolymers ◽  
Self Assembly ◽  
Triblock Copolymers ◽  
Variable Temperature ◽  
Inverse Temperature ◽  
Temperature Transition ◽  
Scanning Calorimetry ◽  
Design Synthesis ◽  
Inverse Temperature Transition ◽  
Functional Biomaterials

AbstractTriblock copolymers have traditionally been synthesized with conventional organic components. However, triblock copolymers could be synthesized by the incorporation of two incompatible protein-based polymers. The polypeptides would differ in their hydrophobicity and confer unique physiochemical properties to the resultant materials. One protein-based polymer, based on a sequence of native elastin, that has been utilized in the synthesis of biomaterials is poly (Valine-Proline-Glycine-ValineGlycine) or poly(VPGVG) [1]. This polypeptide has been shown to have an inverse temperature transition that can be adjusted by non-conservative amino acid substitutions in the fourth position [2]. By combining polypeptide blocks with different inverse temperature transition values due to hydrophobicity differences, we expect to produce amphiphilic polypeptides capable of self-assembly into hydrogels. Our research examines the design, synthesis and characterization of elastin-mimetic block copolymers as functional biomaterials. The methods that are used for the characterization include variable temperature 1D and 2D High-Resolution-NMR, cryo-High Resolutions Scanning Electron Microscopy and Differential Scanning Calorimetry.

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