Morphological observations on liposomes bearing covalently bound protein: studies with freeze-fracture and cryo electron microscopy and small angle X-ray scattering techniques.
The appearance of protein bound to the surface of intact and microfluidized liposomes and its possible influence on their morphology was examined by freeze-fracture electron microscopy, cryo electron microscopy and small angle X-ray scattering (SAXS) techniques. Results obtained by the two microscopy techniques were in agreement with one another in terms of vesicle size and localization of protein (tetanus toxoid or immunoglobulin G) on the surface of vesicles. Surface-bound protein was observed as particles (10-12 nm diameter) by freeze-fracture electron microscopy and was confirmed by immunogold cryo microscopy. SAXS was shown to be a suitable means to further characterize liposomes with, or without bound protein.
Skalko
N
N
Centre for Drug Delivery Research, The School of Pharmacy, University of London, 29-39 Brunswick Square, London WC1N 1AX, UK.
Bouwstra
J
J
Spies
F
F
Stuart
M
M
Frederik
P M
PM
Gregoriadis
G
G
D000818:Animals; D002417:Cattle; D015925:Cryopreservation; D005614:Freeze Fracturing; D007074:Immunoglobulin G / Q000737:chemistry / Q000648:ultrastructure; D008081:Liposomes / Q000737:chemistry*; D016253:Microscopy, Immunoelectron; D010316:Particle Size; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure; D012542:Scattering, Radiation; D013499:Surface Properties; D013745:Tetanus Toxoid / Q000737:chemistry; D014965:X-Rays
D007074:Immunoglobulin G; D008081:Liposomes; D011506:Proteins; D013745:Tetanus Toxoid