Higher order self-assembly of vesicles by site-specific binding.
The association of lipid molecules into spherical vesicles in solution as a result of non-specific intermolecular forces constitutes a primary self-assembly process. Such vesicles can undergo a secondary self-assembly into higher order structures in a controlled and reversible manner by means of site-specific ligand-receptor (biotin-streptavidin) coupling. Cryoelectron microscopy shows these structures to be composed of tethered, rather than adhering, vesicles in their original, unstressed state. In contrast, vesicles aggregated by nonspecific, such as van der Waals, forces are deformed and stressed, producing unstable structures. Vesicle association by site-specific binding provides a practical mechanism for the production of stable, yet controllable, microstructured biomaterials.
Chiruvolu
S
S
Department of Chemical Engineering, University of California, Santa Barbara 93106.
Walker
S
S
Israelachvili
J
J
Schmitt
F J
FJ
Leckband
D
D
Zasadzinski
J A
JA
D000268:Adhesiveness; D001426:Bacterial Proteins / Q000737:chemistry; D001710:Biotin / Q000031:analogs & derivatives / Q000737:chemistry; D003102:Colloids; D005614:Freeze Fracturing; D008051:Lipid Bilayers; D008081:Liposomes / Q000737:chemistry*; D008433:Mathematics; D008854:Microscopy, Electron; D010713:Phosphatidylcholines / Q000737:chemistry; D010714:Phosphatidylethanolamines / Q000737:chemistry; D019809:Streptavidin; D013499:Surface Properties
D001426:Bacterial Proteins; D003102:Colloids; D008051:Lipid Bilayers; D008081:Liposomes; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; C015153:1,2-dilauroylphosphatidylcholine; C007510:1,2-dipalmitoyl-3-phosphatidylethanolamine; D001710:Biotin; C004749:desthiobiotin; D019809:Streptavidin