An Intrinsically Disordered Peptide-Peptide Stapler for Highly Efficient Protein Ligation Bothin Vivoandin Vitro

2018 ◽  
Vol 140 (50) ◽  
pp. 17474-17483 ◽  
Author(s):  
Xia-Ling Wu ◽  
Yajie Liu ◽  
Dong Liu ◽  
Fei Sun ◽  
Wen-Bin Zhang
Keyword(s):  
Protein Ligation ◽  
Intrinsically Disordered ◽  
Highly Efficient ◽  
Intrinsically Disordered Peptide

scholarly journals Does liquid–liquid phase separation drive peptide folding?

2021 ◽  
Author(s):  
Dean N. Edun ◽  
Meredith R. Flanagan ◽  
Arnaldo L. Serrano
Keyword(s):  
Infrared Spectroscopy ◽  
Phase Separation ◽  
Liquid Phase ◽  
Model Membrane ◽  
Peptide Folding ◽  
Two Dimensional ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Peptide ◽  
Two Dimensional Infrared Spectroscopy ◽  
Liquid Liquid Phase Separation

Two-dimensional infrared spectroscopy reveals folding of an intrinsically disordered peptide when sequestered into a model “membrane-less” organelle.

Receptor-templated stapling of intrinsically disordered peptide ligands

2015 ◽  
Vol 13 (14) ◽  
pp. 4183-4189 ◽  
Author(s):  
Conor M. Haney ◽  
W. Seth Horne
Keyword(s):  
Peptide Ligands ◽  
Intrinsically Disordered ◽  
Protein Receptor ◽  
Intrinsically Disordered Peptide ◽  
Peptide Stapling

We report here a method for peptide stapling where a protein receptor guides the reaction by acting as a template that folds a disordered ligand into a bioactive state prior to cyclization.

scholarly journals An Intrinsically Disordered Peptide Facilitates Non-Endosomal Cell Entry

2016 ◽  
Vol 55 (10) ◽  
pp. 3369-3372 ◽  
Author(s):  
Scott H. Medina ◽  
Stephen E. Miller ◽  
Allison I. Keim ◽  
Alexander P. Gorka ◽  
Martin J. Schnermann ◽  
...  
Keyword(s):  
Cell Entry ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Peptide

scholarly journals Order from Disorder with Intrinsically Disordered Peptide Amphiphiles

2021 ◽  
Author(s):  
Guy Jacoby ◽  
Merav Segal Asher ◽  
Tamara Ehm ◽  
Inbal Abutbul-Ionita ◽  
Hila Shinar ◽  
...  
Keyword(s):  
Peptide Amphiphiles ◽  
Stimuli Responsive ◽  
Biochemical Engineering ◽  
Micellar Phase ◽  
Ph Response ◽  
Intrinsically Disordered ◽  
Potential Applications ◽  
Intrinsically Disordered Peptide ◽  
Disordered Peptides

Amphiphilic molecules and their self-assembled structures have long been the target of extensive research due to their potential applications in fields ranging from materials design to biomedical and cosmetic applications. Increasing demands for functional complexity have been met with challenges in biochemical engineering, driving researchers to innovate in the design of new amphiphiles. An emerging class of molecules, namely, peptide amphiphiles, combines key advantages and circumvents some of the disadvantages of conventional phospholipids and block-copolymers. Herein, we present new peptide amphiphiles comprised of an intrinsically disordered peptide conjugated to two variants of hydrophobic dendritic domains. These molecules termed intrinsically disordered peptide amphiphiles (IDPA), exhibit a sharp pH-induced micellar phase-transition from low-dispersity spheres to extremely elongated worm-like micelles. We present an experimental characterization of the transition and propose a theoretical model to describe the pH-response. We also present the potential of the shape transition to serve as a mechanism for the design of a cargo hold-and-release application. Such amphiphilic systems demonstrate the power of tailoring the interactions between disordered peptides for various stimuli-responsive biomedical applications.

scholarly journals Order from Disorder with Intrinsically Disordered Peptide Amphiphiles

2021 ◽  
Author(s):  
Guy Jacoby ◽  
Merav Segal Asher ◽  
Tamara Ehm ◽  
Inbal Abutbul-Ionita ◽  
Hila Shinar ◽  
...  
Keyword(s):  
Peptide Amphiphiles ◽  
Stimuli Responsive ◽  
Biochemical Engineering ◽  
Micellar Phase ◽  
Ph Response ◽  
Intrinsically Disordered ◽  
Potential Applications ◽  
Intrinsically Disordered Peptide ◽  
Disordered Peptides

Amphiphilic molecules and their self-assembled structures have long been the target of extensive research due to their potential applications in fields ranging from materials design to biomedical and cosmetic applications. Increasing demands for functional complexity have been met with challenges in biochemical engineering, driving researchers to innovate in the design of new amphiphiles. An emerging class of molecules, namely, peptide amphiphiles, combines key advantages and circumvents some of the disadvantages of conventional phospholipids and block-copolymers. Herein, we present new peptide amphiphiles comprised of an intrinsically disordered peptide conjugated to two variants of hydrophobic dendritic domains. These molecules termed intrinsically disordered peptide amphiphiles (IDPA), exhibit a sharp pH-induced micellar phase-transition from low-dispersity spheres to extremely elongated worm-like micelles. We present an experimental characterization of the transition and propose a theoretical model to describe the pH-response. We also present the potential of the shape transition to serve as a mechanism for the design of a cargo hold-and-release application. Such amphiphilic systems demonstrate the power of tailoring the interactions between disordered peptides for various stimuli-responsive biomedical applications.

Sign in / Sign up

Export Citation Format

Share Document