Sulfonated Peptide Synthesis (Peptide Sulfonation / Tyrosine Sulfation)

Site-defined, homogeneous sulfonated peptides (commonly referred to as sulfated peptides in biology) with defined modification site(s) and stoichiometry. Use sulfonated PTM peptides to map receptor binding, chemokine interactions, and create reliable assay controls.

Overview

Peptide sulfonation is often used as a practical service keyword for ordering modified peptides. In most biological literature, the dominant PTM is tyrosine sulfation (Tyr‑SO3H), a negatively charged modification that can dramatically change peptide–protein recognition—especially in extracellular signaling, chemokines, and GPCR ligand interactions.

Bio-Synthesis provides custom sulfonated peptide synthesis (peptide sulfonation / tyrosine sulfation, Tyr-SO₃H) as site-defined, homogeneous PTM peptides with controlled modification site(s) and stoichiometry. Our synthetic sulfonated (sulfated) peptides eliminate the heterogeneity typical of biological mixtures and are delivered with purification, LC–MS/HPLC QC, and COA for GPCR and chemokine binding, signaling studies, antibody validation, and assay-grade controls.

Why sulfonated (sulfated) peptides?
  • Introduce a strong negative charge at defined position(s) (Tyr‑SO3H)
  • Model native extracellular PTMs that drive receptor binding
  • Enable cleaner mechanistic interpretation vs mixed modification states
  • Create robust positive/negative controls for binding and functional assays
Common applications
  • GPCR/chemokine receptor binding and competition assays
  • Protein–peptide interaction mapping (site and state dependence)
  • Antibody validation and specificity checks
  • Assay calibration, benchmarking, and negative controls

Related PTM services: PTM hub, acetylated peptides, methylated peptides, and phosphorylated peptides.

Sulfonation types we synthesize (site-defined)

Tyrosine-sulfated peptides (Tyr‑SO3H)

The most common biological form is tyrosine sulfation, typically written as Tyr(SO3H) or pTyr‑sulfate. We synthesize site-defined Tyr‑SO3H peptides for extracellular signaling and binding studies.

  • Single-site Tyr‑SO3H
  • Multi-sulfated motifs (two or more Tyr‑SO3H sites) when biologically relevant
  • Matched unmodified control recommended
Panels and controls (recommended)

Sulfonation effects are often site- and state-dependent. Panels reduce false negatives and help identify the correct binding determinants.

  • Unmodified vs sulfonated matched pairs
  • Single-site variants (each Tyr site individually sulfonated)
  • Multi-site combinations to model native patterns
Quick chooser (60 seconds)
Use “sulfonated / sulfated PTM peptide” when you need…
  • Native extracellular PTM mimicry (Tyr‑SO3H)
  • Receptor/chemokine binding specificity mapping
  • State-defined controls (unmodified vs sulfonated)
  • Clean stoichiometry for reproducible assays
Use “conjugated / functionalized peptide” when you need…
  • Detection labels (fluorescence, FRET)
  • Capture tags (biotin) or immobilization
  • Handles for assembly (azide/alkyne/DBCO click)
  • Solubility/PK tuning (PEG, lipid payloads)

If you’re unsure whether your target uses tyrosine sulfation, share the protein/ligand context and your assay—we’ll recommend the right format and controls.

Sulfonation reference (fast)
Modification Shorthand Charge impact Typical use
Tyrosine sulfation Tyr‑SO3H Strongly negative GPCR/chemokine binding; extracellular recognition; controls
Unmodified tyrosine Tyr Neutral Matched control; specificity comparison

Note: In biology, the standard term is tyrosine sulfation. Many customers search “sulfonated peptides,” so we use both terms for clarity.

SEO note: In biological contexts, these are often called sulfated peptides; many customers search for sulfated peptide synthesis as a synonym for sulfonated peptide synthesis.

Applications

Receptor & chemokine binding

Map sulfation-dependent recognition for GPCR ligands, chemokines, and extracellular signaling interactions.

Specificity mapping

Use site variants to locate the minimal sulfonation motif required for binding or activity.

Assay controls

Matched unmodified controls and sulfonated panels improve reproducibility and reduce ambiguous results.

Why synthetic sulfonated peptides outperform biological mixtures
  • Site-defined modification and homogeneous composition
  • Controlled stoichiometry (single- vs multi-sulfonation)
  • Matched controls (unmodified and site-variant panels)
  • Assay-ready QC and documentation (LC–MS/HPLC + COA)

Design tips

Include these in your request
  • Exact sequence and target Tyr site(s) for Tyr‑SO3H
  • Single-site vs multi-site pattern (if multiple Tyr present)
  • Terminal format (C-terminal acid vs amide)
  • Assay context (binding, competition, functional readout)
Best-practice panels
  • Unmodified vs sulfonated matched pair
  • Single-site variants (each Tyr individually sulfonated)
  • Multi-site combinations to reflect native patterns
  • Optional negative controls (scrambled or site-null variants)

If your target has multiple tyrosines, order a small site-variant panel—it’s the fastest way to identify the binding-critical sulfation site(s).

QC & handling

Quality control deliverables
  • Analytical HPLC chromatogram
  • LC–MS confirmation of expected mass shift
  • Certificate of Analysis (COA)
  • Panel QC notes (on request)
Handling & stability guidance
  • Storage and aliquoting guidance to minimize freeze–thaw
  • Buffer/pH recommendations aligned to your assay
  • Notes for long incubations and sample prep workflows
  • Assay-specific guidance (binding vs LC–MS workflows)

Tip: Share assay buffer, pH, and incubation time so we can recommend formats that preserve modification integrity and reduce redesign cycles.

Ready to order sulfonated (sulfated) peptides?

Get sulfonated peptide synthesis with site-defined Tyr‑SO3H, matched controls, and assay-ready QC (LC–MS/HPLC + COA).

  • Single-site and multi-site Tyr‑SO3H
  • Site-variant panels to pinpoint binding determinants
  • Receptor/chemokine binding and assay controls

Request a Quote

Not sure if your system is sulfation-dependent?

Many extracellular interactions change dramatically with Tyr‑SO3H. Talk with a peptide chemist to choose the right sites, controls, and panel design.

  • Site selection and panel strategy
  • Control design to reduce false negatives
  • Assay-fit QC recommendations

Speak to a Chemist

FAQ

Is “peptide sulfonation” the same as tyrosine sulfation?

In most biological contexts, the canonical PTM is tyrosine sulfation (Tyr‑SO3H). Many customers search “sulfonated peptides,” so we use both terms and clarify the specific modification being synthesized.

Are sulfonated (sulfated) peptides synthetic?

Yes. Research-grade sulfonated/sulfated peptides are typically chemically synthesized so the modification is installed at defined residue positions and stoichiometry. This avoids heterogeneity and supports reproducible binding and functional assays.

Should I order unmodified controls?

Yes. For most studies, we recommend an unmodified matched control plus site variants when multiple tyrosines are present. This isolates the sulfation-dependent contribution to binding or activity.

Can sulfonation be combined with other PTMs or labels?

Often, yes. If you need additional PTMs or workflow handles (e.g., biotin or fluorescence), share your design and we’ll recommend a format that preserves the key sulfation state.

Recommended reading

Background on tyrosine sulfation, extracellular signaling, and binding specificity.

Want a tailored reading list for your receptor/chemokine target? Share your system and we’ll recommend key references and panel designs.

Contact & quote request

Request a quote

Share sequence, sulfonation/sulfation site(s), desired pattern (single vs multi), purity, quantity, and application.

Request a Quote

Talk to a scientist

Need help choosing sites or controls? We’ll recommend an efficient panel design for sulfation-dependent binding or signaling assays.

Contact Bio-Synthesis

Why Choose Bio-Synthesis

Trusted by biotech leaders worldwide for over 40+ years of delivering high quality, fast and scalable synthetic biology solutions.