Self-assembly pathway of peptide nanotubes formed by a glutamatic acid-based bolaamphiphile

2015 ◽  
Vol 51 (58) ◽  
pp. 11634-11637 ◽  
Author(s):  
Emerson Rodrigo da Silva ◽  
Wendel Andrade Alves ◽  
Valeria Castelletto ◽  
Mehedi Reza ◽  
Janne Ruokolainen ◽  
...  

The self-assembly of peptide nanotubes formed by an l-glutamic acid-based bolaamphiphile is shown to proceed via a remarkable mechanism where the peptide conformation changes from β-sheet to unordered.

2010 ◽  
Vol 132 (12) ◽  
pp. 4230-4241 ◽  
Author(s):  
Emilie Pouget ◽  
Nicolas Fay ◽  
Erik Dujardin ◽  
Nadège Jamin ◽  
Patrick Berthault ◽  
...  

2017 ◽  
Vol 56 (20) ◽  
pp. 12652-12663 ◽  
Author(s):  
Shumpei Kai ◽  
Yui Sakuma ◽  
Takako Mashiko ◽  
Tatsuo Kojima ◽  
Masanori Tachikawa ◽  
...  

Soft Matter ◽  
2016 ◽  
Vol 12 (32) ◽  
pp. 6728-6736 ◽  
Author(s):  
Didier Law-Hine ◽  
Mehdi Zeghal ◽  
Stéphane Bressanelli ◽  
Doru Constantin ◽  
Guillaume Tresset

2013 ◽  
Vol 66 (1) ◽  
pp. 23 ◽  
Author(s):  
Soo Jung Son ◽  
Margaret A. Brimble ◽  
Sunghyun Yang ◽  
Paul W. R. Harris ◽  
Tom Reddingius ◽  
...  

The formation of functional liposomes by the self assembly of a peptide–amphiphile that comprises the neuroprotective tripeptide motif glycyl-prolyl-glutamic acid linked to a hydrophobic moiety is reported. The self-assembled peptide–lipid conjugate displays long range order and can be dispersed as nanometre sized particles.


2020 ◽  
Author(s):  
Yuyang Miao ◽  
Shibo Lv ◽  
Daoyuan Zheng ◽  
Yuhan Liu ◽  
Dapeng Liu ◽  
...  

Abstract Porphyrin-based metal coordination polymers (MCPs) have attracted numerous attention due to their great promise application in phototherapy including photodynamic therapy (PDT) and photothermal therapy (PTT). However, the detailed self-assembly process of porphyrin-based MCPs still remains poorly understood. This work provides a detailed study of the self-assembly process of MCPs constructed by Mn2+ and TCPP (TCPP: 4,4′,4′′,4′′′-(Porphine-5,10,15,20-tetrayl)tetrakis(benzoic acid)) in aqueous solution. Unlike traditional nucleation and growth mechanism, we discover that there is a metastable metal-organic intermediate which is kinetically favored in the self-assembly process. And the metastable metal-organic intermediate nanotape structures could convert into thermodynamically favored nanosheets through disassembling into monomers followed by reassembling process. Moreover, the two structurally different assemblies exhibit distinct photophysical performances. The intermediate Mn-TCPP aggregates show good light-induced singlet oxygen 1O2 generation for PDT while the thermodynamic favored stable Mn-TCPP aggregates exhibit good photothermal conversion ability as photothermal agents (PTAs). This study could facilitate controlling self-assembly pathway to fabricate complex MCPs with desirable applications.


2015 ◽  
Vol 10 (8) ◽  
pp. 1684-1689 ◽  
Author(s):  
SeongByeong Park ◽  
Myungsoo Lee ◽  
Seokmin Shin

1996 ◽  
Vol 2 (11) ◽  
pp. 1395-1398 ◽  
Author(s):  
Annie Marquis-Rigault ◽  
Annick Dupont-Gervais ◽  
Alain Van Dorsselaer ◽  
Jean-Marie Lehn

Author(s):  
Theyencheri Narayanan ◽  
Axel Rüter ◽  
Ulf Olsson

This brief report presents an X-ray scattering investigation of self-assembled nanotubes formed by a short peptide. X-ray scattering methods enable multiscale structural elucidation of these nanotubes in solution under the same conditions involved in the self-assembly process. In particular, the dimensions of nanotubes and the crystalline organization within their walls can be determined quantitatively. This is illustrated in the case of amyloid-β(16-22) peptide nanotubes.


2013 ◽  
Vol 750-752 ◽  
pp. 1630-1634
Author(s):  
Li Ping Ruan ◽  
Zhi Hua Xing

In this paper, we reported the dynamic self-assembly process of an half-sequence ionic self-complementarity peptide CH3CO-Pro-Ser-Phe-Cys-Phe-Lys-Phe-Glu-Pro-NH2, which could self-assemble into stable nanofibers and formed hydrogel consisting of >99% water. The dynamic self-assembly process was detected by circular dichroism (CD) and atomic force microscopy (AFM). CD spectrum revealed that the mainly contents of the peptide were regular β-sheet structure. The data indicated that though the secondary structure of the peptide formed immediately, the microstructure of the self-assembly process of the designed peptide formed slowly. AFM image illustrated that the self-assembly process was layer-by-layer assembly.


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