Microgels with tunable affinity-controlled protein release via desolvation of self-assembled peptide nanofibers

2016 ◽  
Vol 4 (18) ◽  
pp. 3054-3064 ◽  
Author(s):  
Margaret M. Fettis ◽  
Yaohua Wei ◽  
Antonietta Restuccia ◽  
Justin J. Kurian ◽  
Shannon M. Wallet ◽  
...  
Keyword(s):  
Protein Binding ◽  
Protein Release ◽  
Peptide Nanofibers ◽  
Self Assembled

We demonstrate an approach to fabricate microgels from self-assembled peptide nanofibers via desolvation. Proteins can be co-desolvated with nanofibers to create protein-loaded microgels. Modifying nanofibers with a protein-binding ligand provides tunable affinity-controlled protein release.

Self-assembled IKVAV peptide nanofibers promote adherence of PC12 cells

2006 ◽  
Vol 26 (5) ◽  
pp. 594-596 ◽  
Author(s):  
Yongchao Wu ◽  
Qixin Zheng ◽  
Jingyuan Du ◽  
Yulin Song ◽  
Bin Wu ◽  
...  
Keyword(s):  
Pc12 Cells ◽  
Peptide Nanofibers ◽  
Self Assembled

Tuning carbohydrate density enhances protein binding and inhibition by glycosylated β-sheet peptide nanofibers

2018 ◽  
Vol 6 (9) ◽  
pp. 2327-2335 ◽  
Author(s):  
Antonietta Restuccia ◽  
Gregory A. Hudalla
Keyword(s):  
Protein Binding ◽  
Binding Affinity ◽  
Binding Proteins ◽  
Carbohydrate Binding ◽  
Peptide Nanofibers ◽  
Carbohydrate Binding Proteins ◽  
Β Sheet

The efficacy of glycosylated β-sheet peptide nanofibers for inhibiting carbohydrate-binding proteins can be increased by tuning carbohydrate density to maximize protein binding affinity.

Artificial peptide-controlled protein release of Zn2+-triggered, self-assembled histidine-tagged protein microparticle

2020 ◽  
Vol 187 ◽  
pp. 110644 ◽  
Author(s):  
Tzu-Yin Chen ◽  
Wan-Jung Cheng ◽  
Jia-Cherng Horng ◽  
Hsin-Yun Hsu
Keyword(s):  
Protein Release ◽  
Self Assembled

Self-Assembled Peptide Nanofibers Encapsulated with Superfine Silver Nanoparticles via Ag+ Coordination

Langmuir ◽  
2015 ◽  
Vol 31 (31) ◽  
pp. 8599-8605 ◽  
Author(s):  
Yuanyuan Hu ◽  
Wenlong Xu ◽  
Guihua Li ◽  
Lu Xu ◽  
Aixin Song ◽  
...  
Keyword(s):  
Silver Nanoparticles ◽  
Peptide Nanofibers ◽  
Self Assembled

Bioinspired Self-Assembled Peptide Nanofibers with Thermostable Multivalent α-Helices

2013 ◽  
Vol 14 (5) ◽  
pp. 1594-1599 ◽  
Author(s):  
So-hee Han ◽  
Mun-kyung Lee ◽  
Yong-beom Lim
Keyword(s):  
Peptide Nanofibers ◽  
Self Assembled

Mineralization of Self-assembled Peptide Nanofibers for Rechargeable Lithium Ion Batteries

2010 ◽  
Vol 22 (48) ◽  
pp. 5537-5541 ◽  
Author(s):  
Jungki Ryu ◽  
Sung-Wook Kim ◽  
Kisuk Kang ◽  
Chan Beum Park
Keyword(s):  
Lithium Ion Batteries ◽  
Lithium Ion ◽  
Peptide Nanofibers ◽  
Self Assembled

Protein-Release Behavior of Self-Assembled PEG-β-Cyclodextrin/PEG-Cholesterol Hydrogels

2009 ◽  
Vol 19 (18) ◽  
pp. 2992-3001 ◽  
Author(s):  
Frank van de Manakker ◽  
Kevin Braeckmans ◽  
Najim el Morabit ◽  
Stefaan C. De Smedt ◽  
Cornelus F. van Nostrum ◽  
...  
Keyword(s):  
Protein Release ◽  
Release Behavior ◽  
Self Assembled

scholarly journals Molecular Mechanics Study of Flow and Surface Influence in Ligand–Protein Association

2021 ◽  
Vol 8 ◽  
Author(s):  
Shivansh Kaushik ◽  
Chia-en A. Chang
Keyword(s):  
Protein Binding ◽  
Brownian Dynamics ◽  
Diffusion Flux ◽  
Hiv Protease ◽  
Self Assembled Monolayer ◽  
Binding Condition ◽  
Protein Association ◽  
Binding Probability ◽  
Self Assembled ◽  
Association Time

Ligand–protein association is the first and critical step for many biological and chemical processes. This study investigated the molecular association processes under different environments. In biology, cells have different compartments where ligand–protein binding may occur on a membrane. In experiments involving ligand–protein binding, such as the surface plasmon resonance and continuous flow biosynthesis, a substrate flow and surface are required in experimental settings. As compared with a simple binding condition, which includes only the ligand, protein, and solvent, the association rate and processes may be affected by additional ligand transporting forces and other intermolecular interactions between the ligand and environmental objects. We evaluated these environmental factors by using a ligand xk263 binding to HIV protease (HIVp) with atomistic details. Using Brownian dynamics simulations, we modeled xk263 and HIVp association time and probability when a system has xk263 diffusion flux and a non-polar self-assembled monolayer surface. We also examined different protein orientations and accessible surfaces for xk263. To allow xk263 to access to the dimer interface of immobilized HIVp, we simulated the system by placing the protein 20Å above the surface because immobilizing HIVp on a surface prevented xk263 from contacting with the interface. The non-specific interactions increased the binding probability while the association time remained unchanged. When the xk263 diffusion flux increased, the effective xk263 concentration around HIVp, xk263–HIVp association time and binding probability decreased non-linearly regardless of interacting with the self-assembled monolayer surface or not. The work sheds light on the effects of the solvent flow and surface environment on ligand–protein associations and provides a perspective on experimental design.

Sign in / Sign up

Export Citation Format

Share Document