Date: 7 July 2026 (Tuesday)
Time: 4:00 pm – 5:00 pm
Venue: Lecture Theatre 1, G/F, William M.W. Mong Block, 21 Sassoon Road 
Host: Professor Cheng-han Yu

Dr. Jing Li is an Assistant Professor in Pediatrics at Harvard Medical School and a Scientist at Boston Children's Hospital. She is a biophysicist whose research focuses on how integrin conformational dynamics regulate cell adhesion, mechanotransduction, and signaling. Dr. Li combines quantitative biophysics, single-molecule imaging, and molecular engineering to investigate integrin activation mechanisms and develop conformation-specific integrin antibodies and ligands. Her work has advanced understanding of integrin energy landscapes, ligand-induced activation, and force-dependent signaling, including pioneering single-molecule FRET studies of integrin activation in collaboration with Taekjip Ha’s group. She has also led the development of integrin subtype–specific antibodies with therapeutic potential. Dr. Li received her Ph.D. in Biophysics from Johns Hopkins University and completed postdoctoral training in Timothy Springer’s group at Boston Children’s Hospital.

Stem cells form organoids in response to extracellular matrix cues, yet the molecular features that determine effective integrin activation remain unclear. Here we combine cryo-electron microscopy, single-molecule measurements, and functional assays to define the principles governing integrin-mediated organoid growth. We determined structures of the bacterial adhesin invasin bound to integrins α5β1 and α6β1, revealing adaptable interactions with diverse α-subunits and an extensive interface with β1 that stabilizes the extended-open (EO) conformation. Across invasin variants and β1-integrin–activating antibodies, we find that all agents bind preferentially to the bent-closed state and induce opening, but differ in their ability to stabilize EO. Strikingly, the fraction of integrins in the EO conformation—rather than binding affinity or kinetics—predicts efficacy in promoting organoid growth. Agents that bind proximal to the ligand-binding pocket and strongly bias EO outperform native matrices when presented as substrates. These findings establish conformational stabilization as a design principle for engineering defined materials for organoid culture and regenerative medicine.

All are welcome.