Regulating the Hydrophobic Domain in Peptide-Catecholamine Coassembled Nanostructures for Fluorescence Enhancement
Ruoyang Zhao, Feng Gao, Maoyu Li, Xingkun Niu, Shihao Liu, Xinmin, Zhao, Liping Wang, Jun Guo, Feng Zhang

TL;DR
This study explores how peptide and catecholamine coassembly modulates hydrophobic nanostructures to enhance fluorescence, providing insights for designing bio-compatible fluorescent probes.
Contribution
It introduces a novel approach to regulate hydrophobic domains in peptide-catecholamine nanostructures for improved fluorescence performance.
Findings
Hydrophobic domain microenvironment controls fluorescence.
Peptide encoding influences nanostructure assembly.
Molecular dynamics simulations support experimental results.
Abstract
Hydrophobic domains provide specific microenvironment for essential functional activities in life. Herein, we studied how the coassembling of peptides with catecholamines regulate the hydrophobic domain-containing nanostructures for fluorescence enhancement. By peptide encoding and coassembling with catecholamines of different hydrophilicities, a series of hierarchical assembling systems were constructed. In combination with molecular dynamics simulation, we experimentally discovered the hydrophobic domain of chromophore microenvironment regulates the fluorescence of coassembled nanostructures. Our results shed light on the rational design of fluorescent bio-coassembled nanoprobes for biomedical applications.
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Taxonomy
TopicsSupramolecular Self-Assembly in Materials · Advanced biosensing and bioanalysis techniques · Nanocluster Synthesis and Applications
