1984
DOI: 10.1016/0005-2736(84)90211-6
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Interaction of antibodies with liposomes bearing fluorescent haptens

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Cited by 38 publications
(21 citation statements)
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“…For liposomes with 10 times less antigen (0.1% biotin), the estimated distance between antigens is 24 nm (assuming 68,000 lipid molecules in the outer leaflet of a 100-nm liposome; Hutchinson et al, 1989), a distance still possible for bivalent binding assuming the hinge region of the antibody is flexible (Amzel and Poljak, 1979;Alzari et al, 1988). However, considering antigen lateral mobility in the bilayer, and that not all liposomal haptens are in a conformation available for binding (Petrossian and Owicki, 1984), bivalent binding would be less for liposomes with a much lower antigen density. This may be the reason for the large difference in antibody consumption between liposomes with 1% biotin and 0.1% biotin observed in the current study (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…For liposomes with 10 times less antigen (0.1% biotin), the estimated distance between antigens is 24 nm (assuming 68,000 lipid molecules in the outer leaflet of a 100-nm liposome; Hutchinson et al, 1989), a distance still possible for bivalent binding assuming the hinge region of the antibody is flexible (Amzel and Poljak, 1979;Alzari et al, 1988). However, considering antigen lateral mobility in the bilayer, and that not all liposomal haptens are in a conformation available for binding (Petrossian and Owicki, 1984), bivalent binding would be less for liposomes with a much lower antigen density. This may be the reason for the large difference in antibody consumption between liposomes with 1% biotin and 0.1% biotin observed in the current study (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…4. Since the rate and strength of the antigen-antibody binding depended on the lipid composition of the vesicles, 11,18) it was apparent that binding was favorable in that membrane.…”
Section: Discussionmentioning
confidence: 99%
“…4, as reported elsewhere. 11,[17][18][19] The relative rate of immunolysis (% release/min) was in the order of II > cholesterol > I >0> III-VI at every molar ratio except for a slightly rise with analogue 0 at molar ratios above 1.0. Increased incorporation of analogue generally resulted in a reduction of the rate of immunolysis except for analogue II, for which the rate remained nearly unchanged up to 1.00 molar addition and decreased slowly above that amount.…”
Section: Effect Of Incorporation Of Analogue II On Antibody-dependentmentioning
confidence: 93%
“…A large number of naturally occurring antibody-antigen interactions involve such recognition and selective binding. Immunogenic responses associated with natural cell membranes have motivated various investigations including studies of artificial lipid membranes [l, 2] either in the form of vesicles [3][4][5][6], or as membranes supported on solid substrates for the development of immunosensors [7][8][9][10][11][12][13].…”
Section: Introductionmentioning
confidence: 99%