Research Progress of Regulation of Driving Forces in Short Peptide Supramolecular Self-Assembly北大核心CSCD

Some short peptides can spontaneously self-assemble into various nanostructures via the synergistic driving forces of non-covalent interactions. These non-covalent interactions，including electrostatic interaction，hydrogen bonding，aromatic interactions and other non-covalent interactions，are usually highly coupled together. Through rational sequence design and proper modification of short peptide molecules，the driving forces could be regulated purposively，and the nanostructures and morphologies of the self-assemblies could be controlled accordingly，and thus so as to achieve the fabrication of peptide-based supramolecular biomaterials and develop their functions. In this paper，the effects of hydrogen bonding，π-π stacking， electrostatic interaction，hydrophobic interaction，metal ion coordination and chiral center on the self-assembly behavior of peptide self-assembly have been reviewed. The driving force regulation strategies， including sequence design，pH and concentration adjustment and metal ion coordination，and the resulted nanostructures have also been discussed. We also make the outlooks on the development of peptide-based supramolecular biomaterials with specific functions in biomedicines and biocatalysis. © 2022, Science Press (China). All rights reserved.

Research Progress of Regulation of Driving Forces in Short Peptide Supramolecular Self?Assembly

Some short peptides can spontaneously self-assemble into various nanostructures via the synergistic driving forces of non-covalent interactions. These non-covalent interactions， including electrostatic interaction， hydrogen bonding， aromatic interactions and other non-covalent interactions， are usually highly coupled together. Through rational sequence design and proper modification of short peptide molecules， the driving forces could be regulated purposively， and the nanostructures and morphologies of the self-assemblies could be controlled accordingly， and thus so as to achieve the fabrication of peptide-based supramolecular biomaterials and develop their functions. In this paper， the effects of hydrogen bonding， π-π stacking， electrostatic interaction， hydrophobic interaction， metal ion coordination and chiral center on the self-assembly behavior of peptide self-assembly have been reviewed. The driving force regulation strategies， including sequence design， pH and concentration adjustment and metal ion coordination， and the resulted nanostructures have also been discussed. We also make the outlooks on the development of peptide-based supramolecular biomaterials with specific functions in biomedicines and biocatalysis.