Abstract:

As widely recognised through last year’s Nobel Prize award, protein design has advanced rapidly and ushered in an era of constructing intricate higher-order protein assemblies. Nonetheless, organising various protein units into artificial higher-order structures similar to biological assembly systems, especially in tubular forms, remains elusive. In this seminar, I will introduce a methodology inspired by nature, which utilises two distinct protein units to create unique tubular structures under carefully designed conditions¹. These structures demonstrate dynamic flexibility and diverse morphologies similar to that of actin filaments and those of microtubules, respectively. By emulating actin filaments, helical conformations are incorporated into the tubular structures, thereby enriching their structural diversity. Notably, these tubular structures can be reversibly disassembled and reassembled in response to environmental stimuli, including changes in salt concentration and temperature, similar to the dynamic behaviour of natural systems. This methodology combines intuitive protein design with biophysical insights, leading to the creation of biomimetic, adaptable, and reversible higher-order protein assemblies. This approach deepens our understanding of protein assembly design, synthetic biology and material science, holding significant implications for unravelling life’s fundamental processes and enabling future applications.
 
¹Noji, M. et al. “Protein design of two-component tubular assemblies similar to cytoskeletons” Nature Communications, 16, 6738 (2025)
https://doi.org/10.1038/s41467-025-62076-3

Speaker: Dr. Masahiro Noji (Kyoto University)
 

 
Host: Naohiro Terasaka, ELSI.

Date: Wed. 22 Oct 16:00-17:00 JST

Venue: Mishima Hall, ELSI (hybrid)