The thickness is based on the mucus containing beads, and as the mucus in IL-10−/− mouse colon is very penetrable, this results in a smaller value than in figure 3B where the mucus thickness is based on charcoal binding to the mucus surface.
Oral administration of these AuNPs-loaded PEDOT/Zn micromotors into the mouse stomach led to their movement in the gastric fluid and binding to the mucus layer on the stomach wall.
Interactions with mucus components were determined within mucus diffusion studies and rheological investigations.
The heterogeneity of mucus components offers a wide range of potential chemical interaction sites for macromolecules, while the mesh-like architecture given to mucus by the intermolecular cross-linking of mucin molecules results in a dense network that physically, and in a size-dependent manner, hinders the diffusion of nanoparticles through mucus.
The mucus components of the gut barrier are fortified by antimicrobial peptides and proteins including lysozyme.
These genes included those categorized as mucus components, mucus-producing cell differentiation-related transcription factors, mucus-producing cell differentiation-related pathways or mediators, post-translational modification of mucin, vesicle transport, ER stress-associated, secretory granule-associated, mucus secretion-related regulators and mucus hypersecretory related ion channels.
In LAB, mucus-binding domains (MUB, MucBP) are found in many proteins and are thought to play a role in binding to the host GI-tract mucus layer [ 57, 93, 94].
Modeling of COREXIT components binding to PPARγ.
Several surface proteins of L. reuteri that are involved in colonisation by binding to epithelia, epithelial cells, or mucus have been functionally characterised [ 12, 15, 19– 21, 53].
Molecular modeling of COREXIT components binding to the PPARγ ligand-binding domain.
