Unknown

Dataset Information

0

An in?situ Dynamic Continuum of Supramolecular Phosphoglycopeptides Enables Formation of 3D Cell Spheroids.


ABSTRACT: Higher-order assemblies of proteins, with a structural and dynamic continuum, is an important concept in biology, but these insights have yet to be applied in designing biomaterials. Dynamic assemblies of supramolecular phosphoglycopeptides (sPGPs) transform a 2D cell sheet into 3D cell spheroids. A ligand-receptor interaction between a glycopeptide and a phosphopeptide produces sPGPs that form nanoparticles, which transform into nanofibrils upon partial enzymatic dephosphorylation. The assemblies form dynamically and hierarchically in?situ on the cell surface, and interact with the extracellular matrix molecules and effectively abolish contact inhibition of locomotion (CIL) of the cells. Integrating molecular recognition, catalysis, and assembly, these active assemblies act as a dynamic continuum to disrupt CIL, thus illustrating a new kind of biomaterial for regulating cell behavior.

SUBMITTER: Wang H 

PROVIDER: S-EPMC5857944 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

An in situ Dynamic Continuum of Supramolecular Phosphoglycopeptides Enables Formation of 3D Cell Spheroids.

Wang Huaimin H   Shi Junfeng J   Feng Zhaoqianqi Z   Zhou Rong R   Wang Shiyu S   Rodal Avital A AA   Xu Bing B  

Angewandte Chemie (International ed. in English) 20171122 51


Higher-order assemblies of proteins, with a structural and dynamic continuum, is an important concept in biology, but these insights have yet to be applied in designing biomaterials. Dynamic assemblies of supramolecular phosphoglycopeptides (sPGPs) transform a 2D cell sheet into 3D cell spheroids. A ligand-receptor interaction between a glycopeptide and a phosphopeptide produces sPGPs that form nanoparticles, which transform into nanofibrils upon partial enzymatic dephosphorylation. The assembli  ...[more]

Similar Datasets

| S-EPMC7284802 | biostudies-literature
| S-EPMC10522563 | biostudies-literature
| S-EPMC4961479 | biostudies-literature
| S-EPMC6270054 | biostudies-literature
2020-11-02 | PXD022297 | Pride
| S-EPMC6214352 | biostudies-literature
| S-EPMC6841729 | biostudies-literature
| S-EPMC6864993 | biostudies-literature
| S-EPMC5376118 | biostudies-literature
| S-EPMC7140689 | biostudies-literature