Publication Date:
1994-06-17
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiruvolu, S -- Walker, S -- Israelachvili, J -- Schmitt, F J -- Leckband, D -- Zasadzinski, J A -- GM47334/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Jun 17;264(5166):1753-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, University of California, Santa Barbara 93106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8209255" target="_blank"〉PubMed〈/a〉
Keywords:
Adhesiveness
;
Bacterial Proteins/chemistry
;
Biotin/analogs & derivatives/chemistry
;
Colloids
;
Freeze Fracturing
;
Lipid Bilayers
;
Liposomes/*chemistry
;
Mathematics
;
Microscopy, Electron
;
Phosphatidylcholines/chemistry
;
Phosphatidylethanolamines/chemistry
;
Streptavidin
;
Surface Properties
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
