TY - JOUR
T1 - Characterization of sonochemically prepared proteinaceous microspheres
AU - Suslick, K. S.
AU - Grinstaff, M. W.
AU - Kolbeck, K. J.
AU - Wong, M.
N1 - Funding Information:
This work was supported by a special creativity extension award from the NSF (CHE-8915020) and the NIH (HL-25934) - M.W.G. gratefully acknowledges receipt of the Procter and Gamble Graduate Fellowship of the Colloid and Surface Chemistry Division of the American Chemical Society. We also thank Lou Ann Miller of UI Veterinary Medicine for her assistance with the TEM micrographs.
PY - 1994/3
Y1 - 1994/3
N2 - Aqueous suspensions of albumin and haemoglobin microspheres can be synthesized using high-intensity ultrasound. The particle size distributions are Gaussian with mean diameters of a few micrometers. These microspheres can contain either nonaqueous liquids (i.e. microcapsules) of air (i.e. microbubbles). The chemical processes involved in the synthesis and some physical properties of the microspheres have been elucidated. Yields and size distributions of albumin microbubbles as a function of experimental parameters indicate that the microspheres are held together primarily by disulphide cross-linking of cysteine residues between protein molecules. The primary oxidizing agent is superoxide (HO2), which is generated from water and oxygen during acoustic cavitation. Physically, the protein within the microsphere shell is not significantly denatured; the heme held within haemoglobin, for example, is fully retained. Optical, scanning electron, and transmission electron microscopy reveals spherical particles with diameters between 1 and 3 μm, and an approximate shell thickness of roughly 30 nm.
AB - Aqueous suspensions of albumin and haemoglobin microspheres can be synthesized using high-intensity ultrasound. The particle size distributions are Gaussian with mean diameters of a few micrometers. These microspheres can contain either nonaqueous liquids (i.e. microcapsules) of air (i.e. microbubbles). The chemical processes involved in the synthesis and some physical properties of the microspheres have been elucidated. Yields and size distributions of albumin microbubbles as a function of experimental parameters indicate that the microspheres are held together primarily by disulphide cross-linking of cysteine residues between protein molecules. The primary oxidizing agent is superoxide (HO2), which is generated from water and oxygen during acoustic cavitation. Physically, the protein within the microsphere shell is not significantly denatured; the heme held within haemoglobin, for example, is fully retained. Optical, scanning electron, and transmission electron microscopy reveals spherical particles with diameters between 1 and 3 μm, and an approximate shell thickness of roughly 30 nm.
KW - albumin microbubbles
KW - microspheres
KW - protein shell
UR - http://www.scopus.com/inward/record.url?scp=0028396891&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028396891&partnerID=8YFLogxK
U2 - 10.1016/1350-4177(94)90030-2
DO - 10.1016/1350-4177(94)90030-2
M3 - Article
AN - SCOPUS:0028396891
SN - 1350-4177
VL - 1
SP - S65-S68
JO - Ultrasonics - Sonochemistry
JF - Ultrasonics - Sonochemistry
IS - 1
ER -