Strategy for self-assembling polypeptides in antitumor applications
The biological activity and high biocompatibility of peptides are advantages for their application as materials,but the presence of endopeptidases,exopeptidases,and kidney filtration functions in vivo limit the antitumor effects of peptides.Based on the presence of non-covalent interactions such as hydrophobic interactions,hydrogen bonds,charge interactions,ππ stacking,and van der Waals forces,peptides can self-assemble into large molecular particles to reduce their own clearance rate in vivo and increase their uptake efficiency by cells.This review analyzes the realization principles underlying peptide self-assembly from the most basic non-covalent forces,hydrogen bonding,and hydrophobic interactions that constitute secondary peptide structures,and elucidates the essential elements required for the construction of self-assembling peptides.This review focuses on the design strategies of self-assembling peptides in recent years,based on the differences between tumor tissues and normal tissues,including acidic microenvironment and various differentially expressed peptide substrate recognition enzymes.In the end,this review provides a prelimina-ry analysis of the current clinical application status of self-assembling peptides,hoping that they can better achieve the transition from laboratory to clinic in the future.
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