Self assembly is an important strategy for nature to construct ordered structures and complex functions , It's also a research hotspot spanning many disciplines in the past 20 years . Self assembly research not only helps to reveal the mysteries of nature , And on this basis, people can learn from nature , The functional materials with novel structures are constructed by self-assembly . In many assembly primitives , The self-assembly of polypeptide molecules has attracted much attention in recent years , In addition to its inherent biocompatibility and biodegradability , It can also be endowed with specific physical and chemical properties and biological functions through reasonable sequence design . Some peptide self-assembly systems are used in tissue engineering 、 regenerative medicine 、 drug release 、 Cancer treatment 、 Biological imaging and other fields have shown potential application value .


Compared with traditional organic small molecules and synthetic polymers , The unique structural characteristics of polypeptide molecules , For example, the repeated arrangement of peptide bonds in the main chain of polypeptide 、 The diversity of side chain functional groups and α- The chirality of carbon , It gives peptides rich interactions between molecules . These assembly drivers include hydrogen bonding 、 Electrostatic action 、 Hydrophobicity 、π-π Interaction 、 Metal ion coordination, etc . Although peptide self-assembly is generally considered as a hierarchical assembly process (hierarchicalself-assembly), But for the role and position of various driving forces in the hierarchical assembly process , And the synergy between them , At present, there is still a lack of a clear understanding , This limits the self-assembly of peptides 、 Effective regulation of assembly structure and function .

lately , China University of petroleum ( East China ) Center for bioengineering and Technology Xu Hai The professor team has made important progress in the study of the synergistic mechanism of peptide self-assembly driving forces and the regulation of hierarchical assembly . They designed a group that contained 28 Of amino acid residues α- Helical peptide , By circular dichroism spectrometer 、 Atomic force microscope 、 Small angle neutron scattering and molecular simulation , Studied α- The hierarchical self-assembly process of helical peptides . The working system shows hydrogen bonding 、 Hydrophobic interaction 、 Electrostatic interaction and metal ion coordination are the four driving forces in the process of peptide self-assembly . Through the reasonable control of different driving forces at different assembly levels , Nano assemblies with different morphologies and structures were obtained . This work provides a general molecular self-assembly model , It can be used to study the self-assembly process of different biomolecules , It is helpful to systematically understand the relationship between self-assembly driving forces and molecular interaction mechanism . Besides , This work also provides strategies for hierarchical construction of biological supramolecular functional systems , Such as the hierarchical assembly of nanofibers 、 Polypeptide assemblies containing metal ion active centers, etc , These structures can be used in the fields of bio functional materials and biomimetic catalysis . Relevant papers are published in Small (DOI:10.1002/smll.202003945) On , And was selected as the current cover article .

With the support of NSFC , Professor Xu Hai and his research team have been devoted to the research of peptide self-assembly and functionalization , Especially the chiral transfer law of self-assembly of short peptides 、 The mechanism of peptide hierarchical assembly and peptide based supramolecular biomaterials .

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