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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Biophys+Rev
2013 ; 5
(2
): 121-136
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Assessment and significance of protein-protein interactions during development of
protein biopharmaceuticals
#MMPMID28510158
Yadav S
; Liu J
; Scherer TM
; Gokarn Y
; Demeule B
; Kanai S
; Andya JD
; Shire SJ
Biophys Rev
2013[Jun]; 5
(2
): 121-136
PMID28510158
show ga
Early development of protein biotherapeutics using recombinant DNA technology
involved progress in the areas of cloning, screening, expression and
recovery/purification. As the biotechnology industry matured, resulting in
marketed products, a greater emphasis was placed on development of formulations
and delivery systems requiring a better understanding of the chemical and
physical properties of newly developed protein drugs. Biophysical techniques such
as analytical ultracentrifugation, dynamic and static light scattering, and
circular dichroism were used to study protein-protein interactions during various
stages of development of protein therapeutics. These studies included
investigation of protein self-association in many of the early development
projects including analysis of highly glycosylated proteins expressed in
mammalian CHO cell cultures. Assessment of protein-protein interactions during
development of an IgG1 monoclonal antibody that binds to IgE were important in
understanding the pharmacokinetics and dosing for this important biotherapeutic
used to treat severe allergic IgE-mediated asthma. These studies were extended to
the investigation of monoclonal antibody-antigen interactions in human serum
using the fluorescent detection system of the analytical ultracentrifuge.
Analysis by sedimentation velocity analytical ultracentrifugation was also used
to investigate competitive binding to monoclonal antibody targets. Recent
development of high concentration protein formulations for subcutaneous
administration of therapeutics posed challenges, which resulted in the use of
dynamic and static light scattering, and preparative analytical
ultracentrifugation to understand the self-association and rheological properties
of concentrated monoclonal antibody solutions.
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