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Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
Published on: September 20, 2017
Hydrophobic affecting in drug-peptide co-assembly: From supramolecular morphology to targeted delivery
Dong Wang1, Zhiqing Zhao1, Hongyang Ma1
1College of Chemistry and Chemical Engineering, China University of Petroleum (East China), Qingdao, Shandong 266580, China.
Abstract:
Traditional drug delivery research emphasizes carrier design, often overlooking the regulatory role of drugs during co-assembly. This study reveals that drug hydrophobicity strongly influences the self-assembly of enzyme-responsive peptides. Two peptides with different hydrophobicity (GR and C₁₂-GR) were tested with four drugs spanning a wide hydrophobicity range (DOX, CCM, CPT, PTX). Drugs with different hydrophobicity solubilize at different positions within the peptide assembly, leading to a transformation in the morphology of the peptide assemblies. These drug-driven changes determined encapsulation efficiency, enzyme-triggered release, and therapeutic outcomes. Cell studies confirmed that optimized drug-carrier combinations enhanced tumor-targeting cytotoxicity with reduced side effects. Overall, the findings highlight drugs as active structural regulators and provide guidance for rational nanomedicine design.
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