Studying the self-assembly of biomolecules not only contributes to understanding cellular functions and the mechanisms of disease onset but also provides effective means for constructing ecologically friendly materials with unique functionalities.
Recently, the team led by Dr. Xuehai Yan, a researcher at the Institute of Process Engineering, Chinese Academy of Sciences, was invited to summarize the research progress of their team in peptide self-assembly and multiscale processes. This includes the discovery of disordered structures resembling droplets, the revelation of a novel mechanism of solvent removal mediated by liquid-liquid phase separation (LLPS) in multistep peptide self-assembly, the development of long-range disordered solid glass materials, and the proposal of key directions for the design and development of the next generation of peptide materials. The relevant work was published in Accounts of Chemical Research and selected as the cover image.
Accounts of Chemical Research Cover Image: Research Team's Contribution
In the fascinating realm of natural molecular self-assembly, both ordered and disordered supramolecular structures emerge ubiquitously, enabling unique biological functions such as molecular recognition and signal transduction. Unlike ordered structures, disordered ones often exist as thermodynamically metastable states, fleeting in their presence and challenging to observe.
Delving deeper, researchers have begun uncovering some disordered structures like condensed droplets or glasses. However, precisely controlling the self-assembly process, especially ensuring the stability and integrity of disordered structures, remains a significant challenge in the peptide self-assembly field.
Led by Dr. Xuehai Yan, the research team has long been dedicated to exploring biomolecular self-assembly, multiscale process mechanisms, and biomedical applications. Building upon previous investigations into ordered structures in peptide self-assembly, the team has devised novel methods to regulate the self-assembly process, facilitating the construction and functional applications of ordered structures.
Furthermore, focusing on transiently occurring droplet-like disordered structures in peptide self-assembly, the team has unveiled a multi-step desolvation process mediated by liquid-liquid phase separation (LLPS), along with new approaches to modulate metastable droplets to obtain ordered structures with diverse morphologies and functionalities.
The team has also discovered long-range disordered solid glass structures in peptide self-assembly, showcasing their advantages in degradability and processability, thereby offering new opportunities for developing novel implantable devices and drug delivery systems.
In their latest published paper, the team further outlines several research directions awaiting exploration in the field of disordered structures in peptide self-assembly. These include combining computer simulations to predict disordered structures, as well as utilizing in-situ imaging and tracking techniques to reveal the properties of disordered structures.
Researchers emphasize that ongoing research and development spanning from ordered to disordered peptide self-assembly processes provide valuable insights for precisely regulating disordered structures and their functional applications. Studies on the formation of condensates by amino acids and peptides through LLPS also offer a method for the development of biomimetic primitive cells, aiding in the understanding of biological evolution processes and the pathogenesis of certain diseases. Additionally, disordered glass structures, owing to their excellent biodegradability, processability, and environmental friendliness, hold promise for widespread applications in biomedical fields such as drug delivery and in wearable devices and other processable device domains.
Dr. Xuehai Yan and Research Officer Ruirui Xing are the co-corresponding authors of this article, with Dr. Rui Chang and Associate Researcher Chengqian Yuan as co-first authors.
For more information on the related paper, visit: http://doi.org/10.1021/acs.accounts.3c00592
