Almost every drug molecule that enters a living system is chemically remodeled before it leaves. Enzymes in the liver and other tissues add oxygen, strip away alkyl groups, cleave esters and amides, or attach polar sugars and sulfate groups, and the products of those reactions are called metabolites. Because a metabolite usually differs from its parent drug in polarity, shape, and biological behavior, it sits at the center of discovery work: it helps explain how a compound is processed in vivo and in vitro, whether an active or a reactive species is formed, and how long the molecule stays in circulation. Yet knowing that a metabolite forms is only half of the problem. Most metabolites appear at very low levels inside complex biological matrices, so the practical challenge is obtaining them as clean, well-characterized compounds that can be weighed, dosed, and quantified. That is where synthesis comes in.
This article moves through the major metabolite families, from oxidative and reductive products to glucuronides, sulfates, and glutathione conjugates, and describes the established synthetic routes that chemists use to prepare each type in useful quantities. Each family is summarized in a comparison table that links the metabolite subtype to its preferred preparation strategy, so that a project team can move quickly from "which metabolite do we need?" to "how should we make it?".
A drug metabolite is the chemical product formed when a biological system transforms a drug molecule. The transformation, called biotransformation, exists for a simple reason: the body needs to convert fat-soluble foreign molecules into more water-soluble forms, via a series of enzymatic reactions, so that they can be excreted. The liver is the principal site of this chemistry, although the gut wall, kidneys, lungs, and plasma also contribute. A small set of enzyme families does most of the work, including cytochrome P450 monooxygenases, flavin-containing monooxygenases, epoxide hydrolases, and hydrolases for the first wave of reactions, followed by transferases such as UDP-glucuronosyltransferases, sulfotransferases, glutathione S-transferases, methyltransferases, and acetyltransferases for the second wave.
The most common way to organize metabolites is by reaction chemistry, which splits them into two great groups. Phase I metabolites are the products of functionalization reactions, in which a polar handle such as a hydroxyl, amino, carboxyl, or thiol group is introduced or uncovered on the skeleton; oxidation dominates this group, but reduction and hydrolysis also belong to it. Phase II metabolites are the products of conjugation reactions, in which a larger, strongly polar endogenous group, such as glucuronic acid, sulfate, glutathione, a methyl group, an acetyl group, or an amino acid, is attached to the molecule. Phase II products are generally more polar than their Phase I precursors and are the forms most often destined for excretion.
Two further classification axes matter just as much when a project team decides what to make. The first is pharmacological behavior: a metabolite may be inactive, contributing little to the parent drug's effect; active, carrying a fraction or even the majority of the pharmacological activity; or reactive, chemically unstable and able to bind cellular macromolecules. The second axis is abundance: metabolites are described as major, minor, or disproportionate according to how much of them is formed relative to the total. These labels change priorities, because a minor metabolite that happens to be reactive can deserve more attention than a major one that is harmless.
Turning this knowledge into usable results depends on having the metabolites in hand. Detecting a peak by liquid chromatography–mass spectrometry is not the same as confirming a structure, and confirming a structure is not the same as being able to weigh out a known amount of the compound. To quantify a metabolite in plasma or to study its activity, scientists need an authentic reference compound with an established identity and a measured purity. When that compound cannot be isolated in sufficient quantity from biological samples, it must be made by synthesis. The sections that follow group the main metabolite types by the reaction that creates them and, for each type, describe how chemists prepare it.
Table.1 The Main Metabolite Classes, Their Structural Change, and Their Typical Synthetic Approach.
| Metabolite Class | Core Structural Change | Representative Enzymes | Common Synthetic Approach |
| Oxidative | Insertion of oxygen: hydroxylation, dealkylation, N-oxidation, sulfoxidation, carboxylation | Cytochrome P450, flavin monooxygenases | Metal-catalyzed C–H oxidation, peracid oxidation, demethylation, carbonyl oxidation |
| Reductive | Addition of hydrogen: carbonyl to alcohol, nitro to amine, azo cleavage, N-oxide reduction | Carbonyl reductases, nitroreductases, azo reductases | Hydride reduction, catalytic hydrogenation, asymmetric reduction |
| Hydrolytic | Cleavage of ester, thioester, amide, or carbamate bonds | Esterases, amidases, epoxide hydrolase | Saponification, amide hydrolysis, independent synthesis of the acid or amine fragment |
| Glucuronide | Attachment of glucuronic acid through O, N, S, or C | UDP-glucuronosyltransferases | Koenigs–Knorr glycosylation, chemoenzymatic glucuronidation |
| Sulfate | Attachment of a sulfate group to a phenol or alcohol | Sulfotransferases | Sulfation with sulfur trioxide complexes, enzymatic sulfation |
| Glutathione conjugate | Addition of glutathione to a soft electrophile | Glutathione S-transferases | Conjugate addition, epoxide opening, sequential peptide trimming |
| Methyl, acetyl, and amino acid conjugates | Attachment of a methyl, acetyl, or amino acid group | Methyltransferases, acetyltransferases, amino acid ligases | Alkylation, acetylation, amide coupling |
Send us the parent structure and the metabolite of interest, and our chemists will propose a route, quantity, and timeline.
Oxidation is the single most productive source of drug metabolites. Cytochrome P450 enzymes insert an oxygen atom into a substrate, and depending on the target they pull it from, the result can be a hydroxyl group on a ring, a hydroxyl group on a chain, the loss of an alkyl group, a new N-oxide or sulfoxide, or a carboxylic acid. Because these reactions are so common, the oxidative family is also the one most often requested as synthesized reference compounds. Preparing an oxidative metabolite usually means either installing the oxygen at the correct position on the parent skeleton or building the oxidized fragment from a simple starting material. The seven subtypes below cover the large majority of cases.
Aromatic hydroxylation adds a hydroxyl group to a phenyl or heteroaromatic ring, converting a benzene ring into a phenol. The position of the new hydroxyl group follows the electronic and steric features of the ring, so the synthetic problem is one of regiochemical control. Chemists approach it in several ways:
Aliphatic hydroxylation places a hydroxyl group on a saturated carbon chain or a benzylic position, producing a primary, secondary, or tertiary alcohol. These metabolites are common on alkyl side chains and on carbons next to aromatic rings, where the C–H bond is chemically weaker. The main synthetic options are:
N-dealkylation removes an alkyl group, most often a methyl or an ethyl, from a nitrogen atom, leaving the parent amine. These metabolites are ubiquitous among drugs that contain a tertiary amine. Two complementary strategies are used:
O-dealkylation cleaves an ether bond between an oxygen and an alkyl group, most commonly converting an aryl methyl ether into a phenol. The synthetic route is essentially a planned demethylation or dealkylation of an ether that already sits at the right position:
N-oxidation converts a tertiary amine into an N-oxide, a polar and weakly basic product that is common for amine-containing drugs. This is one of the most straightforward oxidative metabolites to make, because the reaction is a controlled oxidation of a nitrogen that is already present:
Sulfoxidation converts a sulfur-containing thioether into a sulfoxide and, if oxidation continues, into a sulfone. The sulfoxide metabolite is chiral at sulfur, so the synthetic problem combines chemoselectivity with stereocontrol:
Carboxylic acid metabolites form when a methyl group, a primary alcohol, or an aldehyde is oxidized to a carboxyl group, or when a nitrile is hydrolyzed. This class is important because acids are often the endpoint of several metabolic steps and can change a molecule's charge and solubility dramatically. The most frequent synthetic approaches are:
Table.2 Oxidative Metabolite Subtypes and Their Preferred Synthetic Routes.
| Oxidative Subtype | Structural Change | Preferred Synthesis Route |
| Aromatic hydroxylation | Aryl C–H becomes aryl C–OH | Directed metalation/oxidation, aniline diazotization and hydrolysis, or selective demethylation of an aryl ether. |
| Aliphatic hydroxylation | Alkyl or benzylic C–H becomes C–OH | Selective C–H oxidation, hydroboration–oxidation of an alkene, carbonyl reduction, or biocatalytic hydroxylation. |
| N-dealkylation | Tertiary amine loses an alkyl group | Dealkylation with α-chloroethyl chloroformate or an oxidant, or selective alkylation of the secondary amine. |
| O-dealkylation | Aryl alkyl ether becomes phenol | Demethylation with boron tribromide, hydrogen bromide, trimethylsilyl iodide, or thiolate. |
| N-oxidation | Tertiary amine becomes N-oxide | Controlled peracid or peroxide oxidation, or flavin monooxygenase biocatalysis. |
| Sulfoxidation | Thioether becomes sulfoxide | Periodate, peroxide, or peracid oxidation under controlled conditions, or asymmetric and biocatalytic sulfoxidation. |
| Carboxylic acid formation | Methyl, alcohol, aldehyde, or nitrile becomes carboxyl | Oxidation of alcohol or aldehyde, oxidative cleavage of an alkene, nitrile hydrolysis, or ester hydrolysis. |
From hydroxylated intermediates to N-oxides and sulfoxides, we design a route around your target structure and deliver the compound you need.
Reductive metabolism is less widespread than oxidation, but it is indispensable in specific chemical environments and can dominate under low-oxygen conditions or in the gut. It converts carbonyl groups into alcohols, nitro groups into amines, azo bonds into two amines, and N-oxides back into tertiary amines. A useful theme runs through this whole family: because reduction reverses an oxidation, reductive metabolites are often prepared by applying a reductive method to a precursor that is easy to obtain, sometimes the parent drug itself. Our chemists routinely apply reduction and hydrogenation at small and intermediate scales to supply these compounds.
Alcohol metabolites arise from the reduction of a ketone to a secondary alcohol or an aldehyde to a primary alcohol. They are frequently chiral, and because the two configurations can behave differently, the synthesis often needs to control which one is formed:
Nitro reduction transforms an aromatic or aliphatic nitro group into a primary amine, passing through nitroso and hydroxylamine intermediates. The amine product is a valuable building block in its own right, which means the synthetic toolbox is broad:
Azo reduction cleaves an azo linkage, releasing two aromatic amines. Because the azo bond is uncommon in modern drugs but common in certain dyes and colorants, the metabolites of interest are the two amines produced by cleavage. Preparation focuses on delivering those amines reliably:
N-oxide reduction returns an N-oxide to its parent tertiary amine. It is the reverse of the oxidative N-oxidation reaction described earlier, and it is studied both as a metabolic step and as a route to regenerate the free amine:
Table.3 Reductive Metabolite Subtypes and Their Preferred Synthetic Routes.
| Reductive Subtype | Structural Change | Preferred Synthesis Route |
| Alcohol formation | Ketone or aldehyde becomes alcohol | Hydride reduction with sodium borohydride or lithium aluminum hydride, asymmetric reduction, or ketoreductase biocatalysis. |
| Nitro reduction | Nitro group becomes primary amine | Catalytic hydrogenation, metal–acid reduction, transfer hydrogenation, or controlled partial reduction to the hydroxylamine. |
| Azo reduction | Azo bond splits into two amines | Hydrogenolytic cleavage of the azo bond, direct synthesis of the target amine, or azo reductase biocatalysis. |
| N-oxide reduction | N-oxide returns to tertiary amine | Reduction with triphenylphosphine, zinc in acetic acid, or titanium(III) chloride, or catalytic hydrogenation. |
From nitro reduction to enantiopure alcohols, our team matches the right reduction method to your structure and scale.
Hydrolysis breaks a bond by adding water, splitting one molecule into two fragments. In drug metabolism it acts on esters, thioesters, amides, and carbamates, and it is often the fastest of all biotransformations because hydrolytic enzymes are abundant in blood, liver, and gut. The special feature of this family from a synthesis standpoint is that the "metabolite" is usually one specific fragment of the parent, most often the acid, the amine, or the alcohol. Making that fragment therefore means either performing the hydrolysis on the parent or building the fragment through an independent route. Our laboratory applies both enzyme-catalyzed reaction chemistry and classical hydrolysis to cover this family.
Ester hydrolysis cleaves an ester into a carboxylic acid and an alcohol, and it is one of the most common metabolic reactions for ester-containing drugs. The acid is usually the metabolite of interest, so the goal is to obtain that acid in pure form:
Thioester hydrolysis cleaves the bond between a carbonyl carbon and a sulfur atom, releasing a carboxylic acid and a thiol. Thioesters appear in drug molecules and in natural products, and their hydrolysis products are often reactive and odorous, so careful handling and purification matter:
Amide hydrolysis cleaves the bond between a carbonyl carbon and a nitrogen, giving a carboxylic acid and an amine. Amide bonds are stronger than ester bonds, so this reaction is slower, but it produces two fragments that are both frequently of interest:
Carbamate hydrolysis cleaves the carbamate linkage, typically releasing an amine together with carbon dioxide (CO2) and an alcohol. The amine is normally the metabolite of interest, and it is a valuable intermediate in its own right:
Table.4 Hydrolytic Metabolite Subtypes and Their Preferred Synthetic Routes.
| Hydrolytic Subtype | Structural Change | Preferred Synthesis Route |
| Ester hydrolysis | Ester becomes acid plus alcohol | Saponification of the parent ester, independent synthesis of the acid, or ester re-formation. |
| Thioester hydrolysis | Thioester becomes acid plus thiol | Controlled thioester hydrolysis, assembly from acid and thiol, or direct acid synthesis. |
| Amide hydrolysis | Amide becomes acid plus amine | Acid, base, or enzymatic amide hydrolysis, independent preparation of each fragment, or amide re-formation. |
| Carbamate hydrolysis | Carbamate becomes amine, carbon dioxide, and alcohol | Hydrolysis with decarboxylation, direct amine synthesis, or carbamate re-formation for comparison. |
Whether the target is an acid, an amine, or an alcohol fragment, we prepare and purify the exact hydrolysis product your study requires.
Glucuronidation is the most common conjugation reaction in drug metabolism. An enzyme from the UDP-glucuronosyltransferase family attaches glucuronic acid, a sugar acid derived from glucose, to a suitable handle on the drug molecule. The result is a large, strongly water-soluble metabolite that is easy for the body to excrete. Because glucuronides are highly polar, thermally sensitive, and frequently unstable, they are difficult to isolate from biological samples in useful amounts, and synthesis is the usual way to obtain them. The coupling chemistry, based on sugar chemistry rather than simple functional-group manipulation, draws on our carbohydrate synthesis and glycan synthesis capabilities. Glucuronides are grouped by the atom that carries the linkage.
O-glucuronides form when glucuronic acid is attached to an oxygen, most often the oxygen of a phenol or an alcohol. They are the most common glucuronide type, and their preparation follows established sugar-coupling logic:
Acyl glucuronides attach glucuronic acid to a carboxylic acid through an ester linkage. They are important because they are chemically reactive and can rearrange or bind to proteins, so both their preparation and their handling demand care:
N-glucuronides attach glucuronic acid to a nitrogen atom, most often on an amine or an amide. They occur less frequently than O-glucuronides but are well documented for amine-containing drugs, and their preparation must control which nitrogen is coupled:
S-glucuronides attach glucuronic acid to a sulfur atom, typically from a thiol. They are less common than their oxygen counterparts but appear for sulfur-containing drugs and their metabolites:
C-glucuronides attach glucuronic acid directly to a carbon atom, usually an aromatic or heteroaromatic carbon, through a carbon–carbon bond. This linkage is the most demanding of the glucuronide family, because it cannot be made by the simple ether or ester couplings used for the others:
Table.5 Glucuronide Metabolite Subtypes and Their Preferred Synthetic Routes.
| Glucuronide Subtype | Linkage to Glucuronic Acid | Preferred Synthesis Route |
| O-glucuronide | Through an oxygen (phenol or alcohol) | Koenigs–Knorr glycosylation with a protected donor, enzymatic glucuronidation, or a chemoenzymatic route. |
| Acyl glucuronide | Through an ester on a carboxylic acid | Ester coupling to a protected donor with low-temperature handling, or mild enzymatic preparation. |
| N-glucuronide | Through a nitrogen (amine or amide) | Reductive amination or direct glycosylation of the amine, with protecting groups controlling the site. |
| S-glucuronide | Through a sulfur (thiol) | Glycosylation of the thiol or use of a thioglycoside precursor, under oxidation-controlled conditions. |
| C-glucuronide | Through a carbon (aromatic C–C bond) | C-glycosylation of an aryl metal with a glycosyl donor, or palladium-catalyzed cross-coupling. |
Our sugar chemists prepare O-, N-, S-, and C-glucuronides and deliver them stable, pure, and ready for quantification.
Sulfation attaches a sulfate group to a molecule through the action of sulfotransferases, which transfer a sulfate unit from the cofactor PAPS. Sulfate conjugates are among the most polar metabolites a drug can form, and they are typically minor in abundance because the sulfate donor is limited. They are also thermally labile and can be difficult to isolate, so synthesis is the practical route to reference compounds. The family splits into two groups according to the atom that receives the sulfate.
Phenolic sulfates form when a sulfate group is attached to the oxygen of a phenol. They are the most frequently encountered sulfate metabolites, especially for drugs that also undergo aromatic hydroxylation:
Aliphatic sulfates attach the sulfate group to the oxygen of an alcohol rather than a phenol. They follow the same chemistry as their phenolic counterparts, with a few practical differences:
Table.6 Sulfate Metabolite Subtypes and Their Preferred Synthetic Routes.
| Sulfate Subtype | Structural Change | Preferred Synthesis Route |
| Phenolic sulfate | Aryl oxygen gains a sulfate group | Sulfation with a sulfur trioxide complex or chlorosulfonic acid, or enzymatic sulfation, followed by salt formation. |
| Aliphatic sulfate | Alkyl oxygen gains a sulfate group | Sulfation of the alcohol with a sulfur trioxide complex, or enzymatic sulfation, with low-temperature isolation. |
We prepare phenolic and aliphatic sulfates and deliver them as stable salts that hold up through storage and analysis.
Glutathione conjugation is the body's main defense against reactive, electron-poor molecules. Glutathione, a tripeptide built from glutamic acid, cysteine, and glycine, uses the sulfur of its cysteine unit to attack soft electrophiles, neutralizing them before they can damage the cell. The conjugates that form are therefore markers of reactive metabolite formation, and they are studied closely whenever a molecule carries a structural alert. Preparing these conjugates makes use of peptide synthesis to assemble the glutathione or a close analog, followed by controlled conjugation. The subtypes below follow the way the electrophile is attacked.
Epoxide-derived conjugates form when glutathione opens a strained three-membered epoxide ring, attaching at one of the two carbons. These conjugates are important markers of oxidative stress in drug metabolism:
Michael addition conjugates form when glutathione adds across a carbon–carbon double bond that is activated by a nearby carbonyl, producing a β-thioether. This is the classic reaction of electron-poor alkenes with thiols:
Aromatic glutathione conjugates form when glutathione attacks an aromatic electrophile, such as a reactive arene oxide intermediate or an activated aryl halide, to give an aryl–sulfur linkage. These conjugates document the activation of aromatic rings:
Cysteine conjugates form when the glutathione portion of a conjugate is trimmed down to the cysteine fragment. They represent the next stage in the pathway that eventually leads to the mercapturic acids:
N-acetylcysteine conjugates, also called mercapturic acids, are the final, excreted form of the glutathione pathway. The cysteine conjugate is acetylated on its nitrogen, which makes the compound more stable and easier to excrete:
Table.7 Glutathione and Related Conjugate Subtypes and Their Preferred Synthetic Routes.
| Conjugate Subtype | Structural Change | Preferred Synthesis Route |
| Epoxide-derived conjugate | Epoxide ring opened by glutathione | Epoxide opening with glutathione or a protected cysteine–glycine fragment, with regiochemical control and deprotection. |
| Michael addition conjugate | Activated alkene gains a β-thioether | Base-catalyzed conjugate addition, or stepwise assembly of the sulfur fragment. |
| Aromatic conjugate | Aryl carbon gains a sulfur linkage | Nucleophilic aromatic substitution, metal-catalyzed coupling, or opening of an arene oxide precursor. |
| Cysteine conjugate | Glutathione portion trimmed to cysteine | Direct conjugation with cysteine, or trimming of a glutathione conjugate. |
| N-acetylcysteine conjugate | Cysteine conjugate is acetylated | Acetylation with acetic anhydride or acetyl chloride, or direct conjugation with N-acetylcysteine. |
We assemble glutathione, cysteine, and N-acetylcysteine conjugates with the exact regiochemistry your reactive-metabolite study requires.
Beyond glucuronidation, sulfation, and glutathione conjugation, several other transfer reactions add small polar groups to drug molecules. Methylation, acetylation, and amino acid conjugation are less common but can dominate for particular chemical classes, and each one changes the molecule's charge, size, and behavior in a distinctive way. Because these reactions either attach a very small group or form a simple amide bond, many of them are among the most accessible metabolites to prepare synthetically. Our team draws on amino acids synthesis and routine coupling chemistry to build this group of conjugates.
N-acetylation attaches an acetyl group to a nitrogen, converting a primary amine into an acetamide. It is a common reaction for amines, and the transformation is technically simple to reproduce:
O-methylation attaches a methyl group to an oxygen, usually converting a phenol into an aryl methyl ether. It is the metabolic counterpart of the O-dealkylation reaction discussed earlier:
N-methylation attaches a methyl group to a nitrogen, converting an amine into a methylamine. It changes the basicity and lipophilicity of the molecule and can affect its binding:
S-methylation attaches a methyl group to a sulfur, converting a thiol into a thioether. It is a less common but well-documented conjugation for sulfur-containing compounds:
Glycine conjugation links a carboxylic acid to the amino acid glycine, forming an acyl glycine. It is a major pathway for aromatic acids and gives a very polar, easily excreted product:
Some drugs form conjugates with amino acids other than glycine, including taurine, glutamine, and glutamate. These conjugates broaden the amino acid conjugation family and are built with the same amide-coupling logic:
Table.8 Methyl, Acetyl, and Amino Acid Conjugate Subtypes and Their Preferred Synthetic Routes.
| Conjugate Subtype | Structural Change | Preferred Synthesis Route |
| N-acetylated | Amine becomes acetamide | Acetylation with acetic anhydride or acetyl chloride, or enzymatic acetylation. |
| O-methylated | Phenol becomes aryl methyl ether | Alkylation with methyl iodide or dimethyl sulfate, dimethyl carbonate, or enzymatic methylation. |
| N-methylated | Amine becomes methylamine | Reductive amination, the Eschweiler–Clarke reaction, or direct alkylation. |
| S-methylated | Thiol becomes thioether | Alkylation of the thiol or use of a mild methylating agent, under oxidation control. |
| Glycine conjugate | Acid becomes acyl glycine | Amide coupling of the acid with glycine, an acyl chloride route, or protected glycine coupling. |
| Other amino acid conjugates | Acid becomes acyl amino acid | Amide coupling, an activated ester strategy, and final deprotection. |
We prepare these small-group and amino acid conjugates with the selectivity and purity your downstream analysis depends on.
BOC Sciences brings the synthesis and the analysis of drug metabolites under one roof. Our chemists work across the full range of the metabolite families described in this article, from hydroxylated and dealkylated products to glucuronides, sulfates, and glutathione conjugates, and they design each route around the target structure rather than forcing it into a fixed template. Because a metabolite is only useful once it has been fully understood, every project pairs custom synthesis with the characterization needed to confirm identity and purity, giving development teams a compound they can rely on.
Our core service is the design and preparation of specific metabolites as discrete compounds. A project usually begins with a parent structure and a list of target metabolites, and our chemists then propose routes that balance step count, selectivity, and cost. Phase I targets include hydroxylated, dealkylated, N-oxidized, sulfoxidized, reduced, and hydrolyzed products, while Phase II targets include glucuronides, sulfates, glutathione and cysteine conjugates, and methyl, acetyl, and amino acid conjugates. Routes are optimized for the quantity you actually need, from the milligram scale used for structure confirmation up to gram quantities for activity work, with scale-up available as a project matures. Isotopically labeled versions can be built into the same route when a labeled reference compound is required.
Synthesizing a compound is only the first half of the job; confirming that it is the right compound matters just as much. Our analytical team characterizes every metabolite with a combination of techniques, using NMR testing to establish the skeleton and the position of each new group, and mass spectrometry to confirm molecular weight and fragmentation. When a metabolite is available only in tiny amounts, or when its structure is uncertain, the same team works from biological samples to identify what is present and to guide the synthetic effort. Purification support, including preparative HPLC, ensures that the final material is clean enough for quantitative use.
For many programs the deliverable is not a bulk quantity of a metabolite but a small, well-characterized reference compound that can calibrate an analytical method or confirm a peak in a biological sample. We treat these reference compounds with the same rigor as any other target: the identity is confirmed by multiple techniques, the purity is measured and reported, and the material is supplied with the documentation needed to use it confidently. Whether the need is a single metabolite or a set of related compounds from the same pathway, the work is planned so that the reference materials can be used immediately in downstream studies.
Table.9 Drug Metabolite Synthesis and Analysis Services at BOC Sciences.
| Service Name | Description | Inquiry |
| Drug Metabolites Synthesis | Custom preparation of Phase I and Phase II metabolites, from hydroxylated and dealkylated products to glucuronides, sulfates, and glutathione conjugates. | Inquiry |
| Metabolite Analysis and Identification | Identification and structural confirmation of metabolites in biological samples, integrated with synthesis to close the loop between detection and a defined compound. | Inquiry |
| Reference Compound Synthesis | Small-scale synthesis of well-characterized reference compounds for method calibration, peak confirmation, and quantification support. | Inquiry |
| Stable Isotope Labeling | Synthesis of stable isotope-labeled metabolites for use as internal reference compounds and for tracing metabolic pathways. | Inquiry |
| Structure Characterization | Combined spectroscopic and spectrometric characterization that establishes the identity, purity, and integrity of each synthesized metabolite. | Inquiry |
| LC-MS Testing | Liquid chromatography–mass spectrometry support for metabolite detection, confirmation, and quantification across a wide range of sample matrices. | Inquiry |
From a single reference compound to a full set of Phase I and Phase II metabolites, our chemists will design a route, confirm the structure, and deliver the material you can use with confidence.
If you have any questions or encounter issues on this page, please don't hesitate to reach out. Our support team is ready to assist you.
