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©2023 American Medical Writers Association. All rights reserved.  
ISSN 2163-5315

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ABSTRACT 
Antibody-drug conjugates (ADCs) are currently among the 
fastest growing drug classes in oncology, combining the 
specificity and targeting capabilities of monoclonal anti-
bodies (mAbs) with the potent cytotoxicity of small mole-
cule drugs. Considered the “biological missiles” of cancer 
therapy, ADCs are composed of 3 key elements: (1) a mAb 
framework that selectively binds to an antigen on the tumor 
cell surface, (2) a cytotoxic drug payload, and (3) a chemical 
linker attaching the 2 entities. Because each of these com-
ponents can vary widely among ADCs, the associated drug 
design is relatively complex, with subtle differences leading 
to immense diversity in the overall drug structure and asso-
ciated pharmacological and clinical properties. As medi-
cal communication experts, it is essential to have a basic 
understanding of the various components of ADC design 
and their potential impact on drug efficacy, safety, and 
capability in targeting certain degrees of antigen expression 
and tumor types. This review aims to provide a basic under-
standing of each component related to ADC design and the 
role they play in defining the pharmacological properties of 
a particular ADC.

BACKGROUND
First proposed by Paul Ehrlich in the early 1900s, the foun-
dational concept of a “magic bullet” as a way to selectively 
transport cytotoxic drugs to a specific target tissue has 
become an ever-closer reality, passing through key mile-
stones over the last century.1,2 The development of chemo-
therapy in the 1940s was a first major step in the transition 
from concept to reality.3 However, the lack of high-level 
specificity and targeting capabilities with cytotoxic agents 
led to a high degree of systemic toxicities and has remained 
an ongoing challenge. The advent of hybridoma technology 
and the development of monoclonal antibodies (mAbs) in 
the 1970s established a highly effective method for target-
ing specific antigens expressed on the tumor cell surface.1,4,5 
This led to the development of targeted therapeutics that 

have become an attractive method for improving tumor 
selectivity and reducing the systemic toxicity associated 
with traditional chemotherapy.6 Combining these 2 tech-
nologies enabled the development of the first antibody-drug 
conjugate (ADC). In recent decades, ADCs have become 
a rapidly expanding therapeutic drug class specifically 
designed to overcome the shortfalls associated with chemo-
therapeutic agents.6,7 Currently, there are 13 ADCs that have 
received US Food and Drug Administration approval for 
various hematological and solid tumor cancers.1,8-20

ADC MECHANISM OF ACTION
ADCs are a group of tripartite drugs made up of a tumor- 
specific mAb conjugated via a stable linker to a potent  
cytotoxic payload.21,22 The core concept of an ADC is to use 
the specific recognition between an antibody and antigen 
to selectively deliver cytotoxic drugs to the tumor site, after 
which the payload is released in the tumor via a specific 
release mechanism.23 The general mechanism of action  
for an ADC can vary depending on the inherent design 
(Figure 1, next page).

ADC DESIGN
The clinical success achieved with a particular ADC is con-
tingent upon several key factors: (1) target antigen, (2) anti-
body framework, (3) method of conjugation, (4) chemical 
linker, and (5) cytotoxic payload (Table 1, next page).

 
Target Antigen
To achieve a favorable therapeutic index and reduce the 
potential for off-target toxicity, the selected target anti-
gen should be tumor-specific or tumor-associated with a 
high level of expression in tumor cells and minimal to no 
expression in healthy tissues.24,28 Following ADC binding, 
target antigens should internalize efficiently via endocyto-
sis to enable ADC entry into the cell and subsequent cel-
lular transport and payload release.1,21,29 The target antigen 
should also undergo efficient recycling or replenishment 
on the cell surface with no associated antigen shedding into 

Jason R. Lewis, PharmD, MS, MBA, BCACP  / LRx Precision Health Consulting and Medical Communication  
Services, Nephi, UT

Antibody-Drug Conjugates: Understanding Associated Drug Design 
and Pharmacology

SCIENCE SERIES

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AMWAJournal.org     29Antibody-Drug Conjugates

Figure 1. General mechanism of action of ADCs with and without bystander killing effect.5,21-23 Following introduction of the antibody-drug 
conjugate (ADC) into the plasma circulation by intravenous injection, the target antigen is recognized on the tumor cell surface, leading to 
subsequent binding and formation of an antigen–ADC complex (ADCc). The complex is then internalized via receptor-mediated endocytosis. For 
ADCs with cleavable linker design, some initial release of drug payload may occur prior to internalization. Once inside the cytosol, endosome, or 
lysosome, the chemical characteristics of these environments (eg, low pH, high glutathione/thiol levels, proteolytic enzymes) allow for further 
payload release. In the case of ADCs with noncleavable linker design, compete degradation of the ADC is typically required for payload release. 
The resulting free cytotoxic drug payload then exerts its cellular destruction via a pathway-specific mechanism (eg, microtubule disruption, DNA 
intercalation). Hydrophobic or nonpolar payloads are capable of crossing cell membranes, thereby exerting a so-called bystander effect. The 
bystander killing effect involves the diffusion of free drug across cell membranes from the target tumor cell and into neighboring tumor cells, 
thereby expanding antitumor activity to tumor cells with low or no target antigen expression, or those that are less accessible directly from the 
circulatory system, eg, solid tumor cells. Ag, antigen.

Table 1. Components of ADC Drug Design1,7,25,26Table 1. Components of ADC Drug Design1,7,25,26

Target antigen Antibody framework Method of conjugation Chemical linker Cytotoxic payload

Ideal characteristics
• Highly expressed in tumor cells
• Homogeneous expression in

tumor cells
• Minimal presence in circulation

and healthy cells

Ideal Characteristics
• Minimal cross reactivity with

healthy tissues
• Low immunogenicity
• Strong binding affinity for the

target antigen
• Long PK half-life

Conventional/stochastic
• Lysine sites
• Reduced cysteine sites

Site-specific
• Engineered reactive cysteine

residues
• Disulfide re-bridging
• Unnatural amino acids
• Enzyme assisted ligation
• Glycan remodeling and

glycoconjugation
• pClick technology

Cleavable linkers
Chemically cleavable
• Acid sensitive
• Glutathione sensitive

Enzymatically cleavable
• Peptide based (protease sensitive)
• Β-glucuronide based
• Phosphate based

Noncleavable linkers
• Thioether (SMCC)
• Maleimido propionyl
• Maleimido caproyl

Tubulin Inhibitors
• Auristatins (eg, MMAE, MMAF)
• Maytansinoids (eg, DM1, DM4)
• Tubulysins (eg, tubulysin A)

DNA damaging agents 
• Calicheamicins (eg, ozogamicin)
• Duocarmycins (eg, duocarmazine)
• Pyrrolbenzodiazepines
• Camptothecin analogues (eg,

govitecan, DXd)

Immunomodulators
• TLR agonists
• STING agonists

Abbreviations: Ag, antigen; DM1, mertansine; DM4, ravtansine; DXd, deruxtecan; Fab, fragment antigen binding; Fc, fragment crystallized; MMAE, monomethyl auristatin E; MMAF, monomethyl auristatin F; PK, 
pharmacokinetic; SMCC, sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carbocylate; STING, stimulator of interferon genes; TLR, toll-like receptor.

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AMWAJournal.org     30Antibody-Drug Conjugates

circulation to improve tumor cell targeting and reduce the 
risk of toxicity.30,31 Solid tumors present a challenge in terms 
of both the drug accessibility and intratumoral heterogene-
ity of the target antigen. Therefore, certain characteristics 
of ADC design, such as cleavable linkers or nonpolarized 
payloads, which permit the release or distribution of drug to 
neighboring tumor cells with low or no antigen expression 
(the so-called bystander effect), may be advantageous in 
ADCs targeting these tumor types.31

Antibody Framework
The antibody framework used in the ADC structure is essen-
tial for facilitating selective binding of target antigens and 
can significantly influence the overall efficacy, therapeutic 
index, and pharmacokinetic and pharmacodynamic char-
acteristics of the end drug product.1,21 Ideally, the selected 
mAb should possess a strong binding affinity with high 
target specificity and minimal cross-reactivity with healthy 
tissues.24 The selected mAb should also facilitate efficient 
internalization, demonstrate low immunogenicity, and have 
a long half-life. Among the 5 major subtypes of human anti-
bodies (eg, immunoglobulin [Ig]A, IgD, IgE, IgG, and IgM), 
IgG antibodies are most often used for ADC development 
because of their plasma stability and strong binding affin-
ity for the fragment crystallized (Fc) receptor.1,21,32 Moreover, 
because of their decreased potential for immunogenicity, 
humanized or fully human mAbs are typically favored in 
ADC design as opposed to murine or chimeric mAbs.

Method of Conjugation: Conventional
The method of conjugation in ADC design refers to the 
approach used to connect the linker and payload to the 
mAb framework.1 Historically, conventional conjugation 
methods have been the most widely used in ADC design. 
Conventional conjugation entails either the alkylation or 
acylation of lysine side chains or the reduction of disulfide 
bonds to liberate cysteine residues for conjugation sites.21,33 
Notably, mAbs such as IgG contain a natural abundance of 
lysine (80-100) and cysteine (32-40) residues, which offer 
ideal sites for linker attachment via conventional conjuga-
tion involving coupling reactions.1,27,33-36

 Conventional conjugation using lysine and cysteine 
residues is stochastic. This can lead to heterogeneous mix-
tures of ADC species with varying sites of conjugation and 
drug-to-antibody ratios (DARs), defined as the number of 
drug payloads conjugated to each mAb.37 DARs associated 
with ADCs produced by conventional conjugation methods 
often vary, ranging from 0 to 8 or more.38 DAR-associated 
variability can potentially impact certain ADC character-
istics, such as hydrophobicity, charge, polarity, pharma-
cokinetics, and thermostability of mAbs.38-40 In some cases 

this may result in insufficient stability, causing premature 
payload release and increased potential for off-target toxici-
ties.1 Elevated DARs can also lead to aggregation, increased 
metabolism, or disruptive coupling within the antigen bind-
ing region of the mAb.21,41,42 Because lysine residues are dis-
tributed throughout both heavy and light chain regions of 
the antibody, coupling reactions resulting in payload con-
jugation near antibody–antigen recognition sites could 
interfere with ADC target binding.1,39 Moreover, ADCs with 
cytotoxic payloads conjugated to heavy chain regions of the 
mAb have lower in vivo efficacy compared with light chain 
conjugates.24,44 Consequently, novel site-specific conju-
gation strategies have been developed that produce more 
homogeneous ADC products with favorable pharmacoki-
netic and antigen binding properties.1,37,41

Method of Conjugation: Site-Specific
Site-specific conjugation strategies are categorized accord-
ing to their associated methodology and generally include 
the following: (1) engineered cysteine residues, (2) disulfide 
rebridging, (3) engineered unnatural amino acids, (4) enzy-
matic assisted ligation (5) glycan remodeling/glycoconju-
gation, and (6) proximity-induced antibody conjugation 
method (pClick) technology.1,21,45,46 Site-specific cysteine 
residues are commonly engineered using THIOMAB tech-
nology, which allows specific positioning of conjugation 
sites within both heavy chain and light chain regions of 
the antibody.47 Drug conjugates created using THIOMAB 
technology are typically referred to as THIOMAB-drug 
conjugates and are shown to have improved safety and ther-
apeutic indexes.46

 Disulfide rebridging is a process in which 4 interchain 
disulfide bonds in an IgG antibody are reduced and sub-
sequently treated with a cysteine-selective cross-linking 
reagent.48 This rebridging process enables simultaneous 
reattachment of polypeptide chain and installation of drug 
molecules or function groups that may be further mod-
ified. Genetically encoded unnatural amino acids, such 
as p-acetylphenylalanine and p-azidophenylalanine, are 
other site-specific conjugation methods that have demon-
strated specific advantages in terms of optimizing physical 
properties of the ADC, and improved associated efficacy, 
pharmacokinetic, and safety profiles.41,49 Compared with 
conventional cysteine conjugated ADCs, those using unnat-
ural amino acids for site-specific conjugation demonstrate 
superior in vitro selectivity and efficacy, particularly in low 
antigen expressing tumor cells.50 Enzyme-assisted liga-
tion techniques use enzymes such as transglutaminase to 
conjugate specific amino acid sequences or tags that are 
genetically engineered and artificially induced to express 
in the antibody.1,21,51 Glycan remodeling or glycoconjuga-

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AMWAJournal.org     31Antibody-Drug Conjugates

tion methods exploit naturally-occurring glycosylation sites 
at the N297 residue in the CH2 domain of IgG antibod-
ies.52 However, relative to other site-specific conjugation 
approaches, glycan remodeling has limited control over 
site placement. A site-selective conjugation method using 
pClick has more recently emerged and uses a proximity 
activated crosslinker to covalently attach to a specific anti-
body site, which eliminates the need for additional antibody 
engineering or post-synthesis treatments.53

Chemical Linker
The primary function of chemical linkers in ADC design 
is to effectively bridge the mAb to the cytotoxic drug pay-
load.1 ADC specificity, potency, safety, and overall activity 
are greatly influenced by the associated linker chemis-
try.24 Linkers are generally designed to remain stable in cir-
culation and release the drug payload once the ADC has 
reached the target tumor site.2,24 Chemical linkers com-
monly employed in ADC design are classified into 2 main 
categories: cleavable and noncleavable linkers.1,24

Cleavable Linkers
Cleavable linkers are designed to exploit cancer-specific 
cellular conditions and are generally divided into 3 pri-
mary categories: acid or pH sensitive, glutathione or redox 
sensitive, and enzymatically cleavable (eg, protease sen-
sitive).21,24,28 Acid-sensitive linkers, such as hydrazone, are 
designed to release the drug payload within acidic environ-
ments, such as lysosomal or endosomal cellular compart-
ments, while remaining stable within the blood’s neutral pH 
environment.1,31 Glutathione-sensitive or disulfide linkers 
exploit the high levels of glutathione and other thiols pres-
ent in the cytosol of cancer cells, thereby enabling selec-
tive cleavage of the cytotoxic payload at the tumor site.24,28,54 
Protease sensitive or peptide-based linkers most often 
consist of dipeptide linkers (eg, valine-citrulline), which 
require enzymatic cleavage of peptide bonds for payload 
release.28,31,55 Compared with chemically liable linkers 
(eg, hydrazone and disulfide), peptide-based linker tech-
nologies allow for greater control of drug delivery, with 
improved systemic stability and rapid enzyme-mediated 
release of the drug payload within the target cell.31

Noncleavable Linkers
In contrast with cleavable linkers that rely on tumor-specific 
cellular conditions for payload release, noncleavable linkers 
require internalization via antigen-mediated endocytosis 
and lysosome-mediated proteolytic degradation for payload 
release.24,31,56 Generally, noncleavable linkers are associated 
with greater plasma stability, longer half-lives, and pose a 
reduced risk for off-target side effects. However, the actions 

of ADCs with noncleavable links are typically restricted to 
the target tumor cell. Moreover, amino acid-drug metab-
olites resulting from the drug payload release tend to be 
more hydrophilic and have greater intrinsic polarity, which 
reduces bystander effect. Commonly used noncleavable 
linkers in ADC design include the thioether linker succin-
imidyl-4-(N-maleimidomethyl) cyclohexane-1-carboxylate 
or maleimide moieties, such as maleimdopropionyl and 
maleimdocaproyl.25

Cytotoxic Drug Payload
The drug payloads employed in the design of ADCs are typ-
ically 100 to 1,000 times more potent than the cytotoxic 
agents used in traditional chemotherapy.24,57 Cytotoxic pay-
loads are generally subdivided into 2 main categories: (1) 
DNA-damaging agents, including calicheamicins, duocar-
mycins, pyrrolobenzodiazepines and camptothecin ana-
logues; and (2) anti-tubulin agents, including auristatins, 
maytansinoids, and tubulysins.1,24,28

 Calicheamicins (eg, ozogamicin) were first isolated from 
the actinomycete Micromonospora echinospora in the mid-
1980s, and act by binding the minor groove of DNA, causing 
site-specific, double-stranded DNA breaks.31,58-60 Notably, 
calicheamicins are highly hydrophobic, which limits the 
DAR or number of payload molecules able to be attached 
per mAb. Duocarmycins are potent alkylating compounds 
derived from the bacteria species Streptomyces zelensis. 
Duocarmycin and its derivatives, such as duocarmazine, 
act by binding to and alkylating adenine within the minor 
groove of DNA, leading to subsequent DNA strand cleavage 
and cellular apoptosis.61-64 Pyrrolobenzodiazepine (PBD) 
dimers, such as tesirine, are DNA-damaging agents derived 
from anthramycin, an antitumor antibiotic isolated from 
Streptomyces.65-68 PBD dimers bind the DNA minor groove, 
forming covalent interstrand DNA crosslinks within tumor 
cells that lead to cytotoxicity and cell death.28,69,70 The forma-
tion of crosslinks resulting from PBD activity, which occurs 
rapidly and with minimal DNA distortion, is thought to 
contribute to their persistence and evasion of DNA repair 
mechanisms. Campothecin is a pentacyclic alkaloid iso-
lated from the stem wood of Camototheca acuminata, a tree 
indigenous to China.71-73 Campothecin and its derivatives 
(eg, govitecan, deruxtecan) act by inhibiting topoisomerase 
I enzyme activity, which results in double-stranded DNA 
breaks and subsequent cell death.72-75

 Auristatins commonly used as ADC payloads include 
monomethyl auristatin E and monomethyl auristatin F, 
which are both synthetic analogues of dolastatin 10, a natu-
rally-occurring antimitotic drug isolated from the sea hare 
Dolabella auricularia.28,76,77 Auristatins inhibit tubulin polym-
erization by attaching to the same binding site as vinca alka-

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AMWAJournal.org     32Antibody-Drug Conjugates

loids (eg, vincristine, vinblastine), which are frequently used 
as traditional chemotherapy agents.78-80 Maytansinoids are 
benzoansamacrolides derived from the bark of an African 
shrub, Maytenus ovatus.81 Similar to auristatins, maytansi-
noids bind at or near the vinca-binding site, thereby inhib-
iting microtubule assembly and inducing mitotic arrest.31,82 
Maytansinoids commonly used in ADC design include 
2 thiomethyl derivatives of maytansine: mertansine and 
ravtansine.1,31,83 Tubulysins comprise a family of more 
recently discovered cytostatic peptides isolated from the 
myxobacteria species, Archangium gephyra and Angiococcus 
disciformis, that act by inhibiting microtubule polymerization 
during mitosis, thereby inducing apoptosis.28,84,85

DISCUSSION
Rapid advances in molecular and genomic technologies 
over the last several decades have ushered in a new era of 
precision medicine and led to the increased use of these 
technologies as important clinical tools for the diagnosis, 
classification, and treatment of disease.86 As the use of pre-
cision-based treatment strategies has expanded, biomarker 
testing has become an increasingly important prognostic 
and predictive tool to improve disease management and 
enabled the development of numerous targeted thera-
pies.88,89 The effect of precision-based approaches on the 
treatment landscape has been especially profound in the 
oncology space, as reflected the growing number of bio-
marker-driven clinical trials, which increased from 15% 
in 2000 to 55% in 2018.89 Although targeted therapies have 
led to major improvements in progression-free and over-
all survival, acquired drug resistance has led to associated 
therapeutic limitations and the need for other treatment 
options.86 ADCs in particular represent a unique treatment 
approach that combines precision-based technology used 
in targeted therapy approaches with chemotherapy-based 
strategies using cytotoxic agents with greater potency.
 Since the approval of the first ADC in 2000, continued 
technological advancements have led to an explosion in 
the number of ADCs under clinical development over the 
last few decades. As of 2022, a total of 12 ADCs with 9 asso-
ciated biomarker targets have been approved for use in the 
treatment of both solid tumor and hematological malignan-
cies.7,90 In addition, over 80 ADCs are currently being eval-
uated in clinical trials, suggesting that utilization of these 
novel agents will continue to increase.
 Most recently, the clinical development of novel ADCs 
has had a profound impact on the treatment landscape for 
solid tumors. The DESTINY series of clinical trials, inves-
tigated the human epidermal growth factor receptor 2 
(HER2)-directed ADC, trastuzumab deruxtecan (T-DXd) in 
a number of solid tumor types.91 Resulting data from these 

trials, led to approved indications in HER2-positive meta-
static breast cancer (mBC), HER2-low mBC, and gastric or 
gastroesophageal cancer, as well as accelerated approval 
in non-small cell lung cancer.16,92-95 Notably, DESTINY trial 
data surrounding T-DXd in mBC were not only unprece-
dented, but also transformative, and have played a major 
in reshaping how HER2 expression in tumors is assessed 
and managed. Historically, HER2 expression assessed via 
immunohistochemistry methods has been associated with 
a binary classification, namely HER2-positive or HER2-
negative.96 Early targeted therapies directed toward the 
HER2 receptor only demonstrated efficacy in HER2-positive 
mBC, with no effect in those with HER2-negative status.96 
However, the unique ADC design associated with T-DXd 
and the resulting bystander effect have expanded observed 
therapeutic responses to patients with lower levels of HER2 
expression.97

CONCLUSION
As the incidence of cancer increases worldwide, growing 
demand for safer, more personalized cancer therapies with 
fewer side effects will undoubtedly propel further advances 
in ADC technology. Over the last 5 years alone, 39 clinical 
trials have investigated over 19 ADCs.98,99 Given the pace at 
which ADC therapeutics are being introduced, the need for 
clear and accurate communication of information regard-
ing these sophisticated treatments will also continue to 
grow. We as medical communicators must make it our mis-
sion to educate ourselves and our readers so that they can 
approach the literature critically and make informed deci-
sions about their use.

Acknowledgments
We thank Yuqian Lu, MA, for her design of the accompany-
ing figure and table.

Author declaration and disclosures: The author notes no  
commercial associations that may pose a conflict of interest in 
relation to this article.
Author contact: lrxprecsionhealth@gmail.com

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https://cen.acs.org/pharmaceuticals/biologics/New-day-
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