Antibody Pharmacokinetics and Pharmacodynamics

Lobo, Evelyn D.; Hansen, Ryan J.; Balthasar, Joseph P.

doi:10.1002/jps.20178

Cited by 909Monoclonal and Polyclonal Antibodies ResearchBiosimilars and Bioanalytical MethodsProtein purification and stability

Antibody Pharmacokinetics and Pharmacodynamics

Lobo, Evelyn D., Hansen, Ryan J., Balthasar, Joseph P.·2004·Journal of Pharmaceutical Sciences

DOI 10.1002/jps.20178

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Abstract

The U.S. Food and Drug administration (FDA) has approved several polyclonal antibody preparations and at least 18 monoclonal antibody preparations (antibodies, antibody fragments, antibody fusion proteins, etc.). These drugs, which may be considered as a diverse group of therapeutic proteins, are associated with several interesting pharmacokinetic characteristics. Saturable binding with target antigen may influence antibody disposition, potentially leading to nonlinear distribution and elimination. Independent of antigen interaction, concentration-dependent elimination may be expected for IgG antibodies, due to the influence of the Brambell receptor, FcRn, which protects IgG from catabolism. Antibody administration may induce the development of an endogenous antibody response, which may alter the pharmacokinetics of the therapeutic antibody. Additionally, the pharmacodynamics of antibodies are also complex; these drugs may be used for a wide array of therapeutic applications, and effects may be achieved by a variety of mechanisms. This article provides an overview of many of the complexities associated with antibody pharmacokinetics and pharmacodynamics.

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Elimination of mAbs through the kidney is considered insignificant, since typical mAb molecular weight (150 kDa) is higher than the glomerular filtration threshold (~55 kDa).
“Elimination of mAbs through the kidney is considered insignificant, since typical mAb molecular weight (150 kDa) is higher than the glomerular filtration threshold (∼55 kDa).23”
From Tutorial on monoclonal antibody pharmacokinetics and its considerations in early development (2018) · cites this paper as [23]
At steady state, mAbs generally exhibit a low volume of distribution of 3-8 L, reflecting their confined distribution to the vascular and interstitial spaces because of their size and polarity.
“At steady state, mAbs generally exhibit a low volume of distribution of 3–8 L (Table 3), reflecting their confined distribution to the vascular and interstitial spaces because of their size and polarity.23”
From Tutorial on monoclonal antibody pharmacokinetics and its considerations in early development (2018) · cites this paper as [23]
Nonspecific clearance is considered dose-independent since most therapeutic antibodies at clinically relevant dose levels would fall far below the circulating endogenous IgG levels of ~10 g/ml.
“Nonspecific clearance is considered dose‐independent since most therapeutic antibodies at clinically relevant dose levels would fall far below the circulating endogenous IgG levels of ∼10 g/ml.23”
From Tutorial on monoclonal antibody pharmacokinetics and its considerations in early development (2018) · cites this paper as [23]

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Authors: Lobo, E. D., Hansen, R. J., & Balthasar, J. P.
Affiliations: Eli Lilly (United States) (US)
University at Buffalo, State University of New York (US)
Corresponding author: Balthasar, Joseph P.
ORCID: Balthasar, Joseph P.
Venue: Journal of Pharmaceutical Sciences
Publisher: Elsevier BV
Published: 2004-11
Volume: 93
Issue: 11
Pages: 2645-2668
ISSN: 0022-3549 (ISSN-L)
DOI: 10.1002/jps.20178
OpenAlex: W2062826169
Cited by: 909
References: 149
Citations by year: 2026: 17 · 2025: 23 · 2024: 23 · 2023: 40 · 2022: 39 · 2021: 49 · 2020: 49 · 2019: 51 · 2018: 47 · 2017: 40 · 2016: 38 · 2015: 71 · 2014: 57 · 2013: 60 · 2012: 50
FWCI: 3.76
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Pharmaceutical Sciences (publishedVersion)
PubMed (publishedVersion)
Funders: National Heart, Lung, and Blood Institute (HL67347, R01HL067347)
National Institute of Allergy and Infectious Diseases (AI60687, R01AI060687)
Topics: Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Immunology and Microbiology › Immunology › Biosimilars and Bioanalytical Methods
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Keywords: monoclonal antibodies, polyclonal antibodies, antibody pharmacokinetics, FcRn receptor, saturable binding, nonlinear elimination, therapeutic proteins, antibody fragments, antibody fusion proteins
MeSH terms: Animals, Antibodies, Binding Sites, Antibody, Pharmaceutical Preparations, Humans, Immunoglobulin Fragments

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Antibody Pharmacokinetics and Pharmacodynamics

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