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Updated: Feb 14, 2026
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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
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Narrowing the diversification of supramolecular assemblies by preorganization
Zhongyan Wang1, Chunhui Liang, Yuna Shang
1State Key Laboratory of Medicinal Chemical Biology, Key Laboratory of Bioactive Materials, Ministry of Education, College of Life Sciences, and Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Nankai University, Tianjin 300071, P. R. China. yangzm@nankai.edu.cn.
Chemical Communications (Cambridge, England)
|February 27, 2018
Summary
The precursor peptide structure significantly impacts nanomaterial formation. Nap-YpYY enables uniform nanofibers via enzyme-instructed self-assembly (EISA), unlike other precursors.
Area of Science:
- Supramolecular chemistry
- Materials science
- Biomaterials engineering
Background:
- Peptide self-assembly is crucial for developing advanced nanomaterials.
- Controlling the self-assembly process is key to achieving desired nanostructures.
- Enzyme-instructed self-assembly (EISA) offers a promising route for biomaterial fabrication.
Purpose of the Study:
- To investigate the influence of phosphorylated peptide precursors on the self-assembly of Nap-YYY.
- To determine how precursor structure affects the final nanomaterial properties and hydrogel stability.
- To explore the role of preorganization in EISA for controlled nanomaterial synthesis.
Main Methods:
- Synthesis of three phosphorylated peptide precursors (Nap-YpYY, Nap-pYYY, Nap-YYpY).
- Characterization of nanomaterials formed via enzyme-instructed self-assembly (EISA) at physiological temperature.
- Analysis of hydrogel properties, including uniformity, stability, and nanostructure morphology.
Main Results:
- Nap-YpYY precursor yielded uniform nanofibers in a stable supramolecular hydrogel via EISA.
- Other precursors (Nap-pYYY, Nap-YYpY) resulted in diverse nanostructures and metastable hydrogels with precipitates.
- The preorganization of Nap-YpYY facilitated rapid folding and accelerated hydrogelation kinetics.
Conclusions:
- The choice of phosphorylated peptide precursor is critical for successful EISA and nanomaterial fabrication.
- Nap-YpYY's preorganization property is essential for forming uniform nanofibers in stable hydrogels.
- This study provides a strategy to manipulate peptide self-assembly for controlled nanomaterial design.
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