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Laminin-Dynamic Bonds Enable Multifunctionality in a Biological 2D Network
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DOI：10.1002/adfm.202304268.png)
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Abstract
En 中文
A layer of laminins, assembled on a thin sheet of collagen type IV (Col-IV) forms the backbone of the basal lamina, which controls biological processes such as embryogenesis, tissue homeostasis, and development. Here, the dynamic functions of laminin-111 (Lam-111) in ultrathin films at the air-water interface are investigated. It is shown that the 2D confinement induces polymerization and that expansion via adlayer formation occurs only with extended growth time. The highly robust self-assembly enables the functionalization of surfaces with cross-linked 2D Lam-111 networks of defined thickness using little more than a beaker. The 2D laminin material also displays two dynamic functions required for the maintenance of tissues - the capability for self-renewal and self-healing. By assembling Lam-111 2D networks at the surface of Col-IV sheets, freestanding bilayers closely mimicking the basal lamina can be produced in vitro. There is a marked difference in miPSC spreading and adhesion force between Lam-111 sheets assembled in the presence or absence of Col-IV. These fundamental studies highlight the importance of dynamic functions, encoded into the molecular structure of the building blocks, for the assembly, maintenance, and functioning of the complex material systems found in natural tissues and can provide cues for the molecular design of resilient technical systems. In this work, laminin-111 is self-assembled into ultrathin films at the air-water interface and their capabilities of self-healing, self-renewal, growth, and their ability to provide mechanical support are explored. These films can further be assembled on preformed collagen-IV sheets to create a bilayer mimicking the basal lamina. The bioinstructivity of such bilayers is demonstrated by single-cell adhesion force measurements.image
Keywords:
2D materials
laminin
molecularly programmed materials
multifunctionality
self-assembly
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