Self-assembly of chimeric peptides toward molecularly defined hexamers with controlled multivalent ligand presentation

This work demonstrates a self-assembling peptide strategy to form finite, molecularly defined trigonal bipyramidal-like hexamers which offer control over multivalent ligand display for enhanced tumor targeting. In this work, we report the self-assembly of chimeric peptides in which two distinctly fo...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2020-07, Vol.56 (52), p.7128-7131
Main Authors: Yuan, Xiushuang, Jiang, Linhai, Chen, Weike, Song, Bo, Chen, Wei, Zuo, Xiaobing, Sun, Xiankai, Li, Xiaopeng, Kirshenbaum, Kent, Luo, Shizhong, Dong, He
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Assembling
Biological Transport
Cell Line, Tumor
Collagen - chemistry
Humans
Ligands
Molecular Dynamics Simulation
Nanofibers - chemistry
Optical Imaging
Peptides
Peptides - chemistry
Peptides - metabolism
Protein Conformation
Protein Multimerization
Receptors, Cell Surface - metabolism
Self-assembly
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Summary:This work demonstrates a self-assembling peptide strategy to form finite, molecularly defined trigonal bipyramidal-like hexamers which offer control over multivalent ligand display for enhanced tumor targeting. In this work, we report the self-assembly of chimeric peptides in which two distinctly folded domains can be organized into a finite peptide hexamer with precise control over multivalent ligand presentation and enhanced tumor cell targeting.
ISSN:1359-7345
1364-548X
DOI:10.1039/d0cc02066d