Well-defined biomimetic surfaces to characterize glycosaminoglycan-mediated interactions on the molecular, supramolecular and cellular levels.

摘要: Glycosaminoglycans (GAGs) are ubiquitously present at the cell surface and in extracellular matrix, crucial for matrix assembly, cell-cell cell-matrix interactions. The supramolecular presentation of GAG chains, along with other components, is likely to be functionally important but remains challenging control characterize, both in vivo in vitro. We a method create well-defined biomimetic surfaces that display GAGs, either alone or together ligands, background suppresses non-specific binding. Through design immobilization platform - streptavidin monolayer serves as molecular breadboard attachment various biotinylated ligands set surface-sensitive situ analysis techniques (including quartz crystal microbalance spectroscopic ellipsometry), tailor made tight on biomolecular orientation, density lateral mobility. Analysing interactions between selected (heparan sulphate, HS) HS-binding chemokine CXCL12α (also called SDF-1α), we demonstrate these versatile cellular interaction studies. T-lymphocytes found adhere specifically presenting CXCL12α, when reversibly bound through HS irreversibly immobilized inert surface, even absence any bona fide adhesion ligand. Moreover, which HS-bound intercellular molecule 1 (ICAM-1) synergistically promote adhesion. Our biofunctionalization strategy should broadly applicable functional studies require GAGs cell-surface components.