 Transgenic non-human animals capable of producing heterologous antibodies |
| The design of a transgenic non-human animal that responds to foreign antigen stimulation with a ... |
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| Transgenic non-human animals capable of producing heterologous antibodies |
| As has been discussed supra, it is desirable to produce human immunoglobulins that are reactive ... |
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| Transgenic non-human animals for producing heterologous antibodies |
| As has been discussed supra, it is desirable to produce human immunoglobulins that are reactive ... |
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| Nucleic acids encoding lymphoid CD30 antigen |
| We claim: 1. An isolated nucleic acid molecule comprising a polynucleotide having a sequence ... |
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| Feeding tray for multiwell test apparatus |
| This invention will be described herein with reference to the growing and use of cells on a ... |
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| Neo-tryptophan |
| What is claimed is: 1. A method of making a neurotensin polypeptide containing neo-tryptophan, said ... |
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| Human immunodeficiency virus decoy |
| OF THE INVENTION The present invention has wide application to immunologic procedures and methods ... |
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| Capsid forming and cystein modified chimaeric MS2-coat protein |
| We claim: 1. A modified coat protein capable of forming a capsid which comprises the coat protein ... |
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| Strategically modified hepatitis B core proteins and their derivatives |
| The present invention relates to a strategically modified hepatitis B core (HBc) protein that is ... |
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Enhancement of intracellular delivery and tissue targeting of drugs and genes
| Details |
Inventors: Muzykantov, Vladimir R.; Albelda, Steve M.;
Assignee: Trustees of the University of Pennsylvania (Philadelphia, PA)
Primary Examiner: Rawlings; Stephen L.
Assistant Examiner:
Attorney, Agent or Firm: Licata & Tyrrell P.C.
A method for enhancing intracellular delivery of effector molecules is provided. The method involves modifying selected antibodies with biotin and streptavidin, conjugating these antibodies with an effector molecule, and delivering the conjugated effector to an intracellular target specifically recognized by the antibody. |
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DETAILED DESCRIPTION OF THE INVENTION Streptavidin (SA) is a tetrameric protein possessing four high affinity binding sites for biotin.
Chemical derivatives of biotin developed during the last two decades allow covalent coupling of biotin residues to biomolecules (amino groups, proteins, sugars, lipids, nucleic acids, peptides, etc.
) without loss of their specific biological activity.
SA crosslinks biotinylated molecules and is widely used as a crosslinking agent (Wilchek, M.
and Bayer, E.
Anal.
Biochem.
1988 171:1 32).
SA is non-toxic and induces no harmful side effects in animals and human patients (Hnatowich et al.
J.
Nucl.
Med.
1987 28:1294 1302; Schecter et al.
Int.
J.
Cancer 1991 48:167 172; Rosebrough, S.
F.
and Hartley, D.
F.
J.
Nucl.
Med.
1996 37(8):1380 1384).
Several groups have attempted to use SA and biotinylated antibodies for in vivo applications such as gamma-immunoscintography (Hnatowich et al.
J.
Nucl.
Med.
1987 28:1294 1302) drug-targeting (Bickel et al.
Proc.
Natl.
Acad.
Sci.
1993 90:2618 2622; Muzykantov et al.
Am.
J.
Physiol.
1996 270:L704 713; Muzykantov et al.
Proc.
Natl.
Acad.
Sci.
USA 1996 93:5213 5218; Muzykantov et al.
J.
Pharmacol.
Exp.
Therap.
1996 279:1026 1034) and blood clearance (Taylor et al.
Proc.
Natl.
Acad.
Sci.
USA 1991 88:3305 3309; Marshall et al.
Br.
J.
Cancer 1994 69:502 507).
When considering antibodies that could be used as potential carriers for effectors, work has focused on the pulmonary endothelium.
Binding sites for two particular molecules are found in high concentrations in pulmonary endothelium, platelet endothelial cell adhesion molecule-1, PECAM-1 (Newman, P.
J.
J.
Clin.
Invest.
1997 99(1):3 7; DeLisser et al.
Trends in Cardiovascular Medicine 1997 151:671 677) and thrombomodulin, TM (Kennel et al.
Nucl.
Med.
Biol.
1990 17:193 200).
Therefore, antibodies to these surface antigens would be excellent candidates for targeting drugs or genetic material to the pulmonary endothelium if they could be effectively delivered intracellularly.
Experiments were performed to determine the effect of biotinylation and conjugation with SA on anti-PECAM binding to immobilized purified PECAM (CD31) and PECAM-expressing cells
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