(753d) Biofilm Extracellular Matrix Protein: From Functional Amyloids to Versatile Biomaterials

Biofilms consist of bacteria embedded in a three-dimensional (3D) extracellular matrix (ECM). An essential component of the biofilms ECM are amyloid fibrils formed by self-assembly of bacterial proteins. The functions of both protein monomers and fibers are essential for the formation, survival, and proliferation of bacterial communities. Recent insights into bacterial biofilm matrix structures have shown the importance of amyloid fibers as common building block structures that confer stability to the ECM. Amyloid fibers formed by from phenol-soluble modulins (PSMs) in Staphylococcus aureus (S. aureus) also attracted great attention in the community. These fibers display extreme amyloid polymorphism and play diverse roles in pathogenicity. We utilized the multiscale/multidisciplinary approaches merging computational methods, microscopy, spectroscopy, and microfluid, converging on 3D molecular architecture and functions of S. aureus amyloid proteins, PSMs, within the same range of reconfiguration times and spatial dimensions. Furthermore, we investigated their assemblies under physiological conditions including fluid flow and shear stress, and how their assembly alternate multicellular organization in the scale of complex tissues as biomimetic biomaterials. These findings led us to the design and discovery of versatile biomaterials effectively mimicking the nanoscale components of ECM and interfaces using bio-inspired building blocks. Lastly, the convergent approaches and multidiscipline efforts provide a unique platform to develop, implement, and iteratively improve integrated design protocols applicable to new materials and devices, aiming to advance their applications in healthcare.