Sankaram Mantripragada - San Diego CA, US Richard Thrift - La Mesa CA, US
International Classification:
A61K009/127
US Classification:
424/450000
Abstract:
Physiologically active oil-core particles, and a method of making physiologically active oil-core particles that include a hydrophobic core material, a hydrophobic drug dissolved or suspended in the core material, and a layer of amphipathic lipids surrounding the hydrophobic core. An optional continuous phase can be an oil-immiscible solution. In one aspect, the method involves the use of a volatile solvent that is removed after the formation of the suspension. The suspension can be used substantially as created, or the particles formulated as a solid dosage form. In another aspect, the particles are formed substantially simultaneously with the volatilization of a propellant, for example, by spraying through an atomizing actuator. The resulting particles have superior particle size distribution and yield properties. The method is appropriate for use with physiologic agents that would be sensitive to heating during the encapsulating process, and also allows aseptic processing by filtration without heating the solutions used in processing.
Controlled Release Formulations Of Lipocalin Muteins
Andreas Hohlbaum - Paunzhausen, DE Martin Huelsmeyer - Wolfersdorf, DE Hendrik Gille - Muenchen, DE Sankaram Bhima Mantripragada - Windsor CO, US Kathleen Marie Campbell - Firestone CO, US
The present invention relates to pharmaceutical compositions for the controlled release of lipocalin muteins and conjugates thereof with a moiety selected from the group consisting of a protein, protein domain, peptide, lipid, fatty acid, polysaccharide and/or an organic polymer that comprise said lipocalin mutein of conjugate thereof in combination with a biodegradable polymer. The invention further relates to a method for the controlled delivery of the lipocalin muteins or conjugates thereof, methods for the production of a controlled release formulation and the thus produced formulation. Finally, the invention is directed to the use of the formulations of the invention for the controlled delivery of the lipocalin mutein, for extending the in vivo half-life of the lipocalin mutein, for increasing the bioavailability of the lipocalin mutein, or for decreasing the immunogenic-ity of the lipocalin mutein upon administration to a subject as well as methods for the treatment of a disease or disorder comprising the administration of the formulations of the invention to a subject in need thereof.
Encapsulation Of Nanosuspensions In Liposomes And Microspheres
Rosa Solis - San Diego CA, US Sankaram Mantripragada - San Diego CA, US Pascal Grenier - Kappelen, FR Alain Nhamias - Bartenheim, FR
International Classification:
A61K009/127
US Classification:
424/450000
Abstract:
Sustained release of hydrophobic agents may be achieved by incorporation of the agents into liposomes and microspheres. This is achieved by use of a nanosuspension comprising the hydrophobic agent. The nanosuspension may be used as the aqueous solution in the formation of the liposomes and microspheres.
- Louisville CO, US Kathleen M. Campbell - Firestone CO, US Sankaram Mantripragada - Windsor CO, US
Assignee:
AntriaBio, Inc. - Louisville CA
International Classification:
A61K 9/50 B01J 13/04 B01F 3/08 B01F 13/00
Abstract:
Embodiments of the present technology may include a system for forming an emulsion. The system may include a coiled tube. The coiled tube may have a first end and a second end. The second end may be located at a position higher than the position of the first end. The system may also include a plurality of beads disposed within the coiled tube. The system may further include a first inlet fluidly connected to the coiled tube. The first inlet may be configured to deliver a first fluid to the first end before the second end. In addition, the system may include a second inlet fluidly connected to the coiled tube. The second inlet may be configured to deliver a second fluid to the first end before the second end.
Use Of Hydrophobic Organic Acids To Increase Hydrophobicity Of Proteins And Protein Conjugates
Examples may include a method of making a protein-PEG conjugate salt with increased hydrophobicity. The method may include providing an aqueous protein solution. This aqueous protein solution may include a protein and a pH buffer. The method may also include reacting a polyethylene glycol with the protein to form a protein-PEG conjugate. The method may further include protonating an amino group on the protein-PEG conjugate with a hydrophobic organic acid in an organic phase. The protonation may form the protein-PEG conjugate salt having a hydrophobic anion that increases the hydrophobicity-PEG conjugate salt.
Amine Pegylation Methods For The Preparation Of Site-Specific Protein Conjugates
Examples include a method of making a protein-PEG conjugate. The method may include providing an aqueous protein solution. The aqueous protein solution may include a protein, a pH buffer, and a chelating agent. The chelating agent may be chosen from the group consisting of an aminopolycarboxylic acid, a hydroxyaminocarboxylic acid, an N-substituted glycine, -(2-amino-2-oxocthyl) aminoethane sulfonic acid (BES), and deferoxamine (DEF). The method may also include introducing sodium cyanoborohydride and a methoxy polyethylene glycol aldehyde to the aqueous protein solution. The sodium cyanoborohydride in the methoxy polyethylene glycol aldehyde may have a molar ratio ranging from about 5:1 to about 1.5:1. The method may further include reacting the methoxy polyethylene glycol aldehyde with the protein to form the protein-PEG conjugate. The pH buffer may maintain a pH of the aqueous protein solution ranging from 4.0 to 4.4 during the reaction.
Proteins And Protein Conjugates With Increased Hydrophobicity
Examples may include a method of making a protein-PEG conjugate salt with increased hydrophobicity. The method may include providing an aqueous protein solution. This aqueous protein solution may include a protein and a pH buffer. The method may also include reacting a polyethylene glycol with the protein to form a protein-PEG conjugate. The method may further include protonating an amino group on the protein-PEG conjugate with a hydrophobic organic acid in an organic phase. The protonation may form the protein-PEG conjugate salt having a hydrophobic anion that increases the hydrophobicity-PEG conjugate salt.
Proteins And Protein Conjugates With Increased Hydrophobicity
Examples may include a method of making a protein-PEG conjugate salt with increased hydrophobicity. The method may include providing an aqueous protein solution. This aqueous protein solution may include a protein and a pH buffer. The method may also include reacting a polyethylene glycol with the protein to form a protein-PEG conjugate. The method may further include protonating an amino group on the protein-PEG conjugate with a hydrophobic organic acid in an organic phase. The protonation may form the protein-PEG conjugate salt having a hydrophobic anion that increases the hydrophobicity-PEG conjugate salt.