Spatiotemporal Self-Assembling Peptides Dictates Cancer-Selective Toxicity.

Spatiotemporal Self-Assembling Peptides Dictates Cancer-Selective Toxicity. Biomacromolecules. 2020 Aug 31;: Authors: Jin S, Jeena MT, Jana B, Moon M, Choi H, Lee E, Ryu JH Abstract The intracellular or pericellular self-assembly of amphiphilic peptides is emerging as a potent cancer therapeutic strategy. Achieving self-assembly of amphiphilic peptides inside a cell or cellular organelle is challenging due to the complex cellular environment, which consists of many amphiphilic biomolecules that may alter the self-assembling propensity of the synthetic peptides. Herein, we show that the hydrophobic-hydrophilic balance of the amphiphilic peptides determines the self-assembling propensity, thereby controlling the cell's fate. A series of peptides were designed to target and self-assemble inside the mitochondria of cancer cells. The hydrophobicity of the peptides was tuned by varying their N-terminus capping. Analysis showed that largest hydrophobic peptide self-assembles before reaching the mitochondria and showed no selectivity toward cancer cells, whereas hydrophilic peptides could not self-assemble inside the mitochondria. Optimum balance between hydrophobicity-hydrophilicity is a critical factor for achieving self-assembly inside the mitochondria, thereby providing greater selectivity against cancer cells. PMID: 32865983 [PubMed - as supplied by publisher]
Source: Biomacromolecules - Category: Biochemistry Authors: Tags: Biomacromolecules Source Type: research