University of Colorado

University of Connecticut

Barofold, Inc.

Baxter International Inc.

Baxalta Gmbh

University Technology Corporation

Wyeth

Medimmune Limited

Other

Becton Dickinson and Company Limited

Xeris Pharmaceuticals, Inc.

Soligenix, Inc.

Endo Pharmaceuticals Colorado, Inc.

Pressure Biosciences, Inc.

Sievers, Robert, E.

John Frank Carpenter

Theodore W Randolph

Marc Besman

Michael Pikal

Serguei Tchessalov

Erik Bjornson

Feroz Jameel

Ramesh Kashi

Richard St John

Kimberly Hassett

Pradyot Nandi

Vu Truong-Le

Nicholas W Warne

Binh Pham

Mark C Manning

Robert Seid

Daniel K Schwartz

Matthew B Seefeldt

Lewis P Stratton

Jonathan N Webb

Amber Clausi

Rebecca L Koval

Suchart Chongpraset

Steven J Prestrelski

Jeffrey B Etter

Joseph T Trotter

Robert E Sievers

John Kinzell

Jean-Bernard Hamel

Robert N Brey

Lyndal K Hesterberg

Adrian C Samaniego

Wei-Jie Fang

Amber Haynes Fradkin

John Paul Gabrielson

Scott P Sellers

Serguei University Of Connecticut Tchessalov

The present invention relates generally to the field of immunogenic compositions containing volatile salts. In certain embodiments, compositions and methods disclosed herein relate to producing and using novel combinations to create frozen immunogenic agents bound to adjuvant having improved formulations and improved consistency of distribution of adjuvant for storage and subsequent delivery to a subject in need thereof.

Thermostable vaccine compositions and methods of preparing the same

Compositions relating to thermostable vaccines and methods of preparing the same. Specifically, methods of preparing thermostable vaccines based on a recombinant ricin neurotoxin protein and uses of co-adjuvants to develop a composition capable of eliciting an immune response in a subject.

Thermostable vaccine compositions and methods of preparing same

The delivery of biopharmaceutical and other therapeutic agents parenterally to an animal via a minimally invasive, low pain administration is provided. The agents are delivered to the patient via, e.g., the epidermal, dermal, or subcutaneous layer of the skin in a concentrated form of injectable glucagon that is dissolved in a pharmaceutically acceptable carrier.

Stable glucagon formulations for the treatment of hypoglycemia

A Factor VIII composition formulated without albumin, comprising the following formulation excipients in addition to Factor VIII: 4% to 10% of a bulking agent selected from the group consisting of mannitol, glycine and alanine; 1% to 4% of a stabilizing agent selected from the group consisting of sucrose, trehalose, raffinose, and arginine; 1 mM to 5 mM calcium salt; 100 mM to 300 mM NaCl; and a buffering agent for maintaining a pH of approximately between 6 and 8. Alternatively, the formulation can comprise 2% to 6% hydroxyethyl starch; 1% to 4% of a stabilizing agent selected from the group consisting of sucrose, trehalose, raffinose, and arginine; 1 mM to 5 mM calcium salt; 100 mM to 300 mM NaCl; and a buffering agent for maintaining a pH of approximately between 6 and 8. In a further embodiment, the formulation can comprise: 300 mM to 500 mM NaCl; 1% to 4% of a stabilizing agent selected from the group consisting of sucrose, trehalose, raffinose, and arginine; 1 mM to 5 mM calcium salt; and a buffering agent.

Albumin-free factor VIII formulations

The disclosure provides a method of preparing an immunologically-active adjuvant-bound freeze dried vaccine composition. A specific embodiment provides a stable vaccine composition comprising an aluminum-salt adjuvant, a recombinantneurotoxin protein and a glass-forming agent. These vaccine compositions are useful in the treatment of humans and other animals at risk of infection fromneurotoxin.

Method of preparing an immunologically-active adjuvant-bound dried vaccine composition

The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.

High pressure refolding of protein aggregates and inclusion bodies

The present invention provides methods for reducing and/or evaluating the immunogenic potential of a therapeutic protein preparation. The present invention further provides pharmaceutical compositions of therapeutic proteins and methods of treatment with the same, the compositions having low immunogenic potential and/or improved efficacy. The invention achieves these goals by evaluating therapeutic protein preparations for subvisible protein particulates, which can contribute significantly to the overall immunogenic potential of the protein preparation. Further, by maintaining the content of such subvisible protein particulates to below an immunogenic threshold level, the resulting pharmaceutical composition is less likely to result in a loss of tolerance (e.g., upon repeated administration), thereby improving both the safety and efficacy profile of the therapeutic.

Method for reducing immunogenicity of therapeutic protein compositions

This invention relates to methods for evaluating or inhibiting the aggregation of a protein in an aqueous suspension including organopolysiloxane and medical articles coated with organopolysiloxane containing a protein solution including sugar and a non-ionic surfactant.

Methods for evaluating the aggregation of a protein in a suspension including organopolysiloxane and medical articles coated with organopolysiloxane containing a protein solution

An albumin-free Factor VIII formulation comprising: 4% to 10% of a bulking agent selected from the group consisting of mannitol, glycine and alanine; 1% to 4% of a stabilizing agent selected from the group consisting of sucrose, trehalose, raffinose, and arginine; 1 mM to 5 mM calcium salt; 100 mM to 300 mM NaCl; and a buffering agent. Alternatively, the formulation can comprise 2% to 6% hydroxyethyl starch; 1% to 4% of a stabilizing agent selected from the group consisting of sucrose, trehalose, raffinose, and arginine; 1 mM to 5 mM calcium salt; 100 mM to 300 mM NaCl; and a buffering agent. In a further embodiment, the formulation can comprise: 300 mM to 500 mM NaCl; 1% to 4% of a stabilizing agent selected from the group consisting of sucrose, trehalose, raffinose, and arginine; 1 mM to 5 mM calcium salt; and a buffering agent.

Provided is a pharmaceutical composition involving a concentrated mixture of a precipitated protein and a liquid medium and a method for manufacturing the concentrated mixture. The concentrated mixture is manufacturable by precipitation of a protein with a biocompatible polymer precipitating agent, followed by removal of sufficient liquid to concentrate the resulting mixture to the desired degree. The precipitated protein can be stored for a significant time in the concentrated mixture, such as intermediate between processing stages during manufacture operations.

High-concentration protein formulations and method of manufacture

The present invention discloses improved methods of disaggregating protein aggregates, and refolding denatured proteins, using high pressure. In particular, the present invention provides for the use of agitation, high temperature, 'stepped' depressurization, dialysis and dilution under pressure to increase the speed and extent of aggregate dissolution and protein refolding.

Methods for protein refolding

Growing community of inventors

Littleton, CO, United States of America

John Frank Carpenter