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

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.

scholarly journals Amyloid Self‐Assembly of hIAPP8‐20 via the Accumulation of Helical Oligomers, α‐Helix to β‐Sheet Transition, and Formation of β‐Barrel Intermediates

Small ◽  
2019 ◽  
Vol 15 (18) ◽  
pp. 1805166 ◽  
Author(s):  
Yunxiang Sun ◽  
Aleksandr Kakinen ◽  
Yanting Xing ◽  
Pouya Faridi ◽  
Aparna Nandakumar ◽  
...  
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet

Stabilization of an α Helix by β-Sheet-Mediated Self-Assembly of a Macrocyclic Peptide

2009 ◽  
Vol 121 (9) ◽  
pp. 1629-1633 ◽  
Author(s):  
Yong-beom Lim ◽  
Kyung-Soo Moon ◽  
Myongsoo Lee
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet ◽  
Macrocyclic Peptide

scholarly journals Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy

2017 ◽  
Vol 114 (14) ◽  
pp. 3601-3606 ◽  
Author(s):  
Haiyan Zhao ◽  
Kunpeng Li ◽  
Anna Y. Lynn ◽  
Keith E. Aron ◽  
Guimei Yu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Noncovalent Interactions ◽  
Dna Packaging ◽  
Protein Subunits ◽  
Significant Strength ◽  
Phage Dna ◽  
Mortise And Tenon ◽  
Α Helix ◽  
Β Sheet ◽  
Protein Shell

The enormous prevalence of tailed DNA bacteriophages on this planet is enabled by highly efficient self-assembly of hundreds of protein subunits into highly stable capsids. These capsids can stand with an internal pressure as high as ∼50 atmospheres as a result of the phage DNA-packaging process. Here we report the complete atomic model of the headful DNA-packaging bacteriophage Sf6 at 2.9 Å resolution determined by electron cryo-microscopy. The structure reveals the DNA-inflated, tensed state of a robust protein shell assembled via noncovalent interactions. Remarkable global conformational polymorphism of capsid proteins, a network formed by extended N arms, mortise-and-tenon–like intercapsomer joints, and abundant β-sheet–like mainchain:mainchain intermolecular interactions, confers significant strength yet also flexibility required for capsid assembly and DNA packaging. Differential formations of the hexon and penton are mediated by a drastic α–helix-to-β–strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses.

Self-Assembly of Recombinant Hagfish Thread Keratins Amenable to a Strain-Induced α-Helix to β-Sheet Transition

2015 ◽  
Vol 16 (8) ◽  
pp. 2327-2339 ◽  
Author(s):  
Jing Fu ◽  
Paul A. Guerette ◽  
Ali Miserez
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet

scholarly journals Peptide Self‐Assembly: Amyloid Self‐Assembly of hIAPP8‐20 via the Accumulation of Helical Oligomers, α‐Helix to β‐Sheet Transition, and Formation of β‐Barrel Intermediates (Small 18/2019)

Small ◽  
2019 ◽  
Vol 15 (18) ◽  
pp. 1970093 ◽  
Author(s):  
Yunxiang Sun ◽  
Aleksandr Kakinen ◽  
Yanting Xing ◽  
Pouya Faridi ◽  
Aparna Nandakumar ◽  
...  
Keyword(s):  
Self Assembly ◽  
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

Stabilization of an α Helix by β-Sheet-Mediated Self-Assembly of a Macrocyclic Peptide

2009 ◽  
Vol 48 (9) ◽  
pp. 1601-1605 ◽  
Author(s):  
Yong-beom Lim ◽  
Kyung-Soo Moon ◽  
Myongsoo Lee
Keyword(s):  
Self Assembly ◽  
Α Helix ◽  
Β Sheet ◽  
Macrocyclic Peptide
Sign in / Sign up

Export Citation Format

Share Document