scholarly journals Presentation of RGDS Epitopes on Self-Assembled Nanofibers of Branched Peptide Amphiphiles

2006 ◽  
Vol 7 (6) ◽  
pp. 1855-1863 ◽  
Author(s):  
Mustafa O. Guler ◽  
Lorraine Hsu ◽  
Stephen Soukasene ◽  
Daniel A. Harrington ◽  
James F. Hulvat ◽  
...  
Keyword(s):  
Peptide Amphiphiles ◽  
Self Assembled

Probing Membrane Hydration at the Interface of Self-Assembled Peptide Amphiphiles Using Electron Paramagnetic Resonance

2018 ◽  
Vol 7 (10) ◽  
pp. 1261-1266 ◽  
Author(s):  
Ian R. Smith ◽  
Alban H. R. Charlier ◽  
Amanda M. Pritzlaff ◽  
Alexander Shishlov ◽  
Brooke Barnes ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Peptide Amphiphiles ◽  
Paramagnetic Resonance ◽  
Self Assembled ◽  
Electron Paramagnetic

Glutathione-adaptive peptide amphiphile vesicles rationally designed using positionable disulfide-bridges for effective drug transport

2020 ◽  
Vol 11 (28) ◽  
pp. 4547-4556
Author(s):  
Hayeon Kim ◽  
Inhye Kim ◽  
Jun Ho Hwang ◽  
Jaehyun Park ◽  
Hyungju Ahn ◽  
...  
Keyword(s):  
Drug Release ◽  
Tumor Cells ◽  
Drug Transport ◽  
Drug Loading ◽  
Effective Drug ◽  
Peptide Amphiphiles ◽  
Disulfide Bridges ◽  
Peptide Amphiphile ◽  
Disulfide Linkages ◽  
Self Assembled

The drug loading/releasing capability of GSH-responsive nanovesicles self-assembled from peptide amphiphiles was controlled by varying the location and number of disulfide-linkages in the peptide for the selective drug-release into tumor cells.

scholarly journals Self-assembled peptide amphiphiles function as multivalent binder with increased hemagglutinin affinity

2013 ◽  
Vol 13 (1) ◽  
pp. 51 ◽  
Author(s):  
Christine Hüttl ◽  
Cornelia Hettrich ◽  
Reinhard Miller ◽  
Bernd-Reiner Paulke ◽  
Petra Henklein ◽  
...  
Keyword(s):  
Peptide Amphiphiles ◽  
Self Assembled

The internal structure of self-assembled peptide amphiphiles nanofibers

Soft Matter ◽  
2007 ◽  
Vol 3 (4) ◽  
pp. 454 ◽  
Author(s):  
Hongzhou Jiang ◽  
Mustafa O. Guler ◽  
Samuel I. Stupp
Keyword(s):  
Internal Structure ◽  
Peptide Amphiphiles ◽  
Self Assembled

scholarly journals Self-assembled micro-fibres by oxime connection of linear peptide amphiphiles

2019 ◽  
Vol 17 (7) ◽  
pp. 1984-1991 ◽  
Author(s):  
Richard Booth ◽  
Ignacio Insua ◽  
Ghibom Bhak ◽  
Javier Montenegro
Keyword(s):  
Self Assembly ◽  
Aqueous Media ◽  
Peptide Amphiphiles ◽  
Linear Peptide ◽  
Self Assembled

The oxime connection between linear peptides and hydrophobic aldehydes affords amphiphiles that are excellent biocompatible scaffolds for the hierarchical self-assembly of nano and micro fibrillar structures in aqueous media.

scholarly journals A combined experimental and computational approach reveals how aromatic peptide amphiphiles self-assemble to form ion-conducting nanohelices

2020 ◽  
Vol 4 (10) ◽  
pp. 3022-3031
Author(s):  
Yin Wang ◽  
Yaxin An ◽  
Yulia Shmidov ◽  
Ronit Bitton ◽  
Sanket A. Deshmukh ◽  
...  
Keyword(s):  
Ionic Conductivity ◽  
Computational Approach ◽  
High Ionic Conductivity ◽  
Peptide Amphiphiles ◽  
Self Assembled ◽  
Ion Conducting

Salt-triggered conversion of nanoribbons into nanohelices was studied experimentally and computationally, revealing unexpectedly high ionic conductivity in these self-assembled nanomaterials.

Designer aromatic peptide amphiphiles for self-assembly and enzymatic display of proteins with morphology control

2019 ◽  
Vol 55 (5) ◽  
pp. 640-643 ◽  
Author(s):  
Rie Wakabayashi ◽  
Ayumi Suehiro ◽  
Masahiro Goto ◽  
Noriho Kamiya
Keyword(s):  
Self Assembly ◽  
Morphology Control ◽  
Peptide Amphiphiles ◽  
Fibrous Materials ◽  
Self Assembled ◽  
Post Modification

Aromatic peptide amphiphiles self-assembled into fibrous materials with varied morphologies and enzymatic post-modification of the materials with proteins was achieved.

scholarly journals Self-Assembled Nanostructures of Peptide Amphiphiles: Charge Regulation by Size Regulation

2019 ◽  
Vol 123 (28) ◽  
pp. 17606-17615 ◽  
Author(s):  
Gervasio Zaldivar ◽  
Sridhar Vemulapalli ◽  
Venkatareddy Udumula ◽  
Martin Conda-Sheridan ◽  
Mario Tagliazucchi
Keyword(s):  
Peptide Amphiphiles ◽  
Size Regulation ◽  
Charge Regulation ◽  
Self Assembled

scholarly journals Self-Assembled Multi-Epitope Peptide Amphiphiles Enhance the Immune Response against Enterovirus 71

Nanomaterials ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 2342
Author(s):  
Yu-Gyeong Kim ◽  
Yunsu Lee ◽  
Joo Hee Kim ◽  
Sun-Young Chang ◽  
Jong-Wha Jung ◽  
...  
Keyword(s):  
Immune Response ◽  
Genetic Material ◽  
Enterovirus 71 ◽  
Host Cells ◽  
Peptide Amphiphiles ◽  
Serum Samples ◽  
Fatty Acid Chain ◽  
Self Assembled ◽  
Cellular Immune ◽  
Chain Lengths

Subunit vaccines consist of non-genetic material, such as peptides or proteins. They are considered safe because they have fewer side effects; however, they have low immunogenicity when used alone. We aimed to enhance the immune response of peptide-based vaccines by using self-assembled multimeric peptide amphiphiles (PAs). We designed two epitope PAs by conjugating epitope peptides from Enterovirus 71 (EV71) virus particle (VP) 1 and VP3 capsid proteins with different fatty acid chain lengths (VP1PA and VP3PA). These PAs self-assembled into supramolecular structures at a physiological pH, and the resulting structures were characterized using atomic force microscopy. Multi-epitope PAs (m-PAs) consisted of a 1:1 mixture of VP1PA and VP3PA solutions. To evaluate immunogenicity, m-PA constructs were injected with adjuvant subcutaneously into female Balb/c mice. Levels of antigen-specific immunoglobulin G (IgG) and IgG1 in m-PA-injected mice serum samples were analyzed using ELISA and Western blotting. Additionally, cytokine production stimulated by each antigen was measured in splenocytes cultured from immunized mice groups. We found that m-PA showed improved humoral and cellular immune responses compared to the control and peptide groups. The sera from m-PA immunized mice group could neutralize EV71 infection and protect host cells. Thus, self-assembled m-PAs can promote a protective immune response and can be developed as a potential platform technology to produce peptide vaccines against infectious viral diseases.

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