Production of particles of therapeutic proteins at the air-water interface during compression/dilation cycles
Particles in protein therapeutics are undesirable because they may have the potential for causing adverse immunogenicity in patients. Agitation-induced exposure to the air-water interface during manufacturing, shipping, and administration can cause particle formation in therapeutic protein products....
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| Published in | Soft matter Vol. 8; no. 4; pp. 1329 - 1335 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
01.01.2012
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Particles in protein therapeutics are undesirable because they may have the potential for causing adverse immunogenicity in patients. Agitation-induced exposure to the air-water interface during manufacturing, shipping, and administration can cause particle formation in therapeutic protein products. We systematically studied how application of surface pressure during periodic interfacial compressions caused a model monoclonal antibody to form particles. Above a critical interfacial compression ratio of 5 we observed a dramatic increase in the rate of protein particle formation. During continuous interfacial compression/dilation cycles, particle numbers increased but the particle size distribution remained unchanged. When cyclic compressions were halted, particles did not nucleate additional particles or grow further in bulk solution suggesting that they are formed only at the air-water interface. In fact, we found that particles in the bulk slowly decreased in number upon standing. The rate of particle formation was only weakly dependent on both the bulk protein concentration and the period of cyclical interfacial compressions. These observations are consistent with the interfacial aggregation of proteins during periods of high surface pressure, followed by collapse of the adsorbed layer and detachment of protein particles from the interface into the bulk.
Non-propagating monoclonal antibody particles formed exclusively at the air-water interface were caused by high surface pressure applied during interfacial compressions. |
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| AbstractList | Particles in protein therapeutics are undesirable because they may have the potential for causing adverse immunogenicity in patients. Agitation-induced exposure to the air-water interface during manufacturing, shipping, and administration can cause particle formation in therapeutic protein products. We systematically studied how application of surface pressure during periodic interfacial compressions caused a model monoclonal antibody to form particles. Above a critical interfacial compression ratio of 5 we observed a dramatic increase in the rate of protein particle formation. During continuous interfacial compression/dilation cycles, particle numbers increased but the particle size distribution remained unchanged. When cyclic compressions were halted, particles did not nucleate additional particles or grow further in bulk solution suggesting that they are formed only at the air-water interface. In fact, we found that particles in the bulk slowly decreased in number upon standing. The rate of particle formation was only weakly dependent on both the bulk protein concentration and the period of cyclical interfacial compressions. These observations are consistent with the interfacial aggregation of proteins during periods of high surface pressure, followed by collapse of the adsorbed layer and detachment of protein particles from the interface into the bulk. Particles in protein therapeutics are undesirable because they may have the potential for causing adverse immunogenicity in patients. Agitation-induced exposure to the air-water interface during manufacturing, shipping, and administration can cause particle formation in therapeutic protein products. We systematically studied how application of surface pressure during periodic interfacial compressions caused a model monoclonal antibody to form particles. Above a critical interfacial compression ratio of 5 we observed a dramatic increase in the rate of protein particle formation. During continuous interfacial compression/dilation cycles, particle numbers increased but the particle size distribution remained unchanged. When cyclic compressions were halted, particles did not nucleate additional particles or grow further in bulk solution suggesting that they are formed only at the air-water interface. In fact, we found that particles in the bulk slowly decreased in number upon standing. The rate of particle formation was only weakly dependent on both the bulk protein concentration and the period of cyclical interfacial compressions. These observations are consistent with the interfacial aggregation of proteins during periods of high surface pressure, followed by collapse of the adsorbed layer and detachment of protein particles from the interface into the bulk. Non-propagating monoclonal antibody particles formed exclusively at the air-water interface were caused by high surface pressure applied during interfacial compressions. |
| Author | Carpenter, John F Stevenson, Jennifer L Bee, Jared S Randolph, Theodore W Schwartz, Daniel K Trabelsi, Siwar Freund, Erwin |
| AuthorAffiliation | Drug Product & Device Development University of Colorado Health Sciences Center Amgen Inc Department of Chemical and Biological Engineering Department of Pharmaceutical Sciences University of Colorado |
| AuthorAffiliation_xml | – name: Amgen Inc – name: Department of Pharmaceutical Sciences – name: University of Colorado – name: Department of Chemical and Biological Engineering – name: University of Colorado Health Sciences Center – name: Drug Product & Device Development |
| Author_xml | – sequence: 1 givenname: Jared S surname: Bee fullname: Bee, Jared S – sequence: 2 givenname: Daniel K surname: Schwartz fullname: Schwartz, Daniel K – sequence: 3 givenname: Siwar surname: Trabelsi fullname: Trabelsi, Siwar – sequence: 4 givenname: Erwin surname: Freund fullname: Freund, Erwin – sequence: 5 givenname: Jennifer L surname: Stevenson fullname: Stevenson, Jennifer L – sequence: 6 givenname: John F surname: Carpenter fullname: Carpenter, John F – sequence: 7 givenname: Theodore W surname: Randolph fullname: Randolph, Theodore W |
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| Snippet | Particles in protein therapeutics are undesirable because they may have the potential for causing adverse immunogenicity in patients. Agitation-induced... |
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| SubjectTerms | Agglomeration Collapse Compressing Dilation Monoclonal antibodies Particle size distribution Proteins Surface pressure |
| Title | Production of particles of therapeutic proteins at the air-water interface during compression/dilation cycles |
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