Peptide–Enzyme Conjugation Services

Enzyme-safe chemistries for controlled peptide attachment and reproducible characterization

peptide–enzyme conjugates
enzyme labeling
site-defined attachment
linker & spacer design
program-aligned QC

Overview

Peptide–enzyme conjugates are widely used in analytical and diagnostic formats because they combine catalytic signal generation with targeting or affinity functions. Established enzyme conjugation strategies and reporting formats are documented in the bioconjugation literature (e.g., Hermanson, Bioconjugate Techniques).

Bio-Synthesis provides custom peptide–enzyme conjugation services using enzyme-compatible chemistries and practical attachment strategies (site-defined or controlled labeling), followed by purification and analytical verification aligned to your application and program stage. These chemically defined peptide–enzyme conjugates often used for diagnostics, assays, and biosensor workflows—with controlled attachment, purification, and documentation aligned to your program stage.

Branched peptide synthesis schematic showing a lysine branching core with two to eight peptide arms (MAP-2, MAP-4, MAP-8) and dendrimer for multivalent epitope presentation.

Typical workflow for peptide–enzyme conjugate synthesis, purification, and analytical control.

Scope note: This page focuses on chemistry, workflow, purification, and analytical qualification. Enzyme activity retention is application-dependent and is discussed as a design consideration rather than a guaranteed outcome.

Related services: Peptide Modifications, Click Chemistry Peptides, Oligonucleotide Conjugation.

Why peptide–enzyme conjugation?

  • Detection of enzyme activity: peptides can introduce affinity tags, spacers, or immobilization handles to improve assay configuration and signal control.
  • Improve enzyme selectivity (context-dependent): targeting or affinity peptides can bias enzyme localization or proximity in engineered assay formats.
  • Expand enzyme applications: diagnostic assays, biosensors, imaging readouts, and surface-based detection.
  • Hybrid constructs: peptide components can support multivalent presentation or modular assembly designs.

Design choices emphasize attachment site, linker/spacer architecture, and reaction conditions to reduce steric interference and preserve enzyme function.

Applications

Immunoassays & diagnostics

Enzyme reporters (e.g., HRP/ALP) coupled to peptides for capture, spacing, or amplification concepts.

  • ELISA-style formats
  • Amplification systems
  • Activity readouts
Biosensors & surfaces

Peptide handles support oriented tethering, spacing, or surface attachment for reproducible sensor builds.

  • Surface-based detection
  • Immobilized enzyme platforms
  • Microfluidic assays
Research tools

Peptide–enzyme conjugates for method development, binding studies, and controlled labeling workflows.

  • Assay development
  • Protein interaction workflows
  • Functional screening

Enzymes and protein systems we conjugate

We support peptide conjugation to common enzyme reporters and enzyme-based systems used in analytical and diagnostic workflows. Additional targets can be evaluated based on structure, reactive residue availability, and intended readout.

Enzymes
  • Horseradish Peroxidase (HRP)
  • Alkaline Phosphatase (ALP)
  • Alkaline Phosphatase Amplification (AMP)
  • Penicillinase (PNC)
  • α-D-Galactosidase
  • Glucose-6-Phosphate Dehydrogenase
Systems & immunoconjugates
  • Biotin–Avidin / Biotin–Streptavidin systems
  • Other enzyme immunoconjugates
  • Non-enzyme protein immunoconjugates

If you have a specific enzyme/protein not listed, share the target and constraints—we’ll recommend a practical attachment plan.

Conjugation chemistry (enzyme-compatible options)

Cys-selective coupling

Used when a defined cysteine handle is available or engineered to support site-defined attachment.

  • Thiol–maleimide strategies
  • Alternative thiol chemistries (design-dependent)
  • Spacer tuning to reduce sterics
Copper-free click

A common route for clean, chemoselective coupling with minimal side reactions.

  • Azide–DBCO / azide–BCN
  • Defined stoichiometry
  • Good analytical clarity
Controlled Lys coupling

Used for enzyme labeling workflows when site-defined handles are constrained.

  • Amine-reactive coupling (design-dependent)
  • Condition control to limit over-labeling
  • Purification and profiling to manage mixtures
Enzyme activity preservation considerations
  • Attachment site planning: avoid active-site and critical binding regions when possible.
  • Spacer selection: PEG or flexible spacers can reduce steric interference.
  • Condition selection: buffers, pH, and reaction time are chosen to protect enzyme stability.

We can align conjugation design to your assay format (solution-phase vs immobilized) and reporting needs.

Typical workflow

Process overview
  1. Design review
    – enzyme selection, peptide sequence, attachment site, and buffer constraints.
  2. Peptide synthesis
    – site-defined handle or controlled labeling strategy.
  3. Enzyme preparation
    – conditioning and buffer exchange for conjugation compatibility.
  4. Conjugation & purification
    – controlled coupling and removal of unconjugated components.
  5. Analytical QC
    – identity confirmation and conjugation profile verification.
Branched peptide synthesis schematic showing a lysine branching core with two to eight peptide arms (MAP-2, MAP-4, MAP-8) and dendrimer for multivalent epitope presentation.

Typical workflow for peptide–enzyme conjugate synthesis, purification, and analytical control.

QC & typical deliverables

Identity
  • Mass spectrometry (method-appropriate)
  • Conjugation verification
Purity / profile
  • Chromatography as appropriate
  • Conjugation profile review (method-dependent)
Documentation
  • COA aligned to program stage
  • Traceable documentation package (program-dependent)

Activity assays can be discussed as a program-specific requirement; analytical verification focuses on identity and conjugation profile.

Our Quality Commitment

Bio-Synthesis is committed to Total Quality Management (TQM) to assure customer satisfaction. Analytical checks are performed following peptide synthesis and peptide–enzyme conjugation, and purification/QA procedures are applied to support consistent quality.

Our quality system follows ISO 9001–aligned practices, with release criteria and documentation scaled to the intended use and program stage.

Last updated: 2026-01-31

Contact & quote request

For the fastest quote, send the enzyme/protein target, peptide sequence and attachment preference (or constraints), preferred chemistry (or “recommend”), and quantity/purity targets.

Fastest path
Request a Quote Conjugation chemistry
Fast quote checklist
  • Enzyme/protein target (HRP, ALP, etc.)
  • Peptide sequence + defined attachment site/handle
  • Preferred chemistry (click / thiol / controlled labeling) or “recommend”
  • Quantity + purity target + intended use
  • Any constraints (buffer, stabilizers, assay format)

Not sure which route fits your constraints? Send target + peptide + constraints—we’ll propose an enzyme-compatible plan.

FAQ

Can enzyme activity be preserved after peptide conjugation?

Conjugation design emphasizes attachment site planning, spacer selection, and enzyme-compatible reaction conditions to reduce steric interference. Retained activity is enzyme- and design-dependent.

Do you support site-defined peptide–enzyme conjugates?

Yes. When a defined handle is available (e.g., cysteine- or click-based), site-defined attachment can be used to improve conjugate homogeneity and analytical clarity.

Which enzymes can be conjugated?

Common targets include HRP, ALP/AMP systems, penicillinase, α-D-galactosidase, glucose-6-phosphate dehydrogenase, biotin–avidin systems, and other enzyme or protein immunoconjugates.

What QC is provided for peptide–enzyme conjugates?

Identity is confirmed by mass spectrometry, and purity or conjugation profiles are assessed by chromatographic methods as appropriate. Documentation and release criteria can be aligned to the intended use and program stage.

Recommended reading

Selected peer-reviewed references describing peptide–enzyme conjugation, enzyme labeling strategies, and bioconjugation principles relevant to analytical, diagnostic, and biosensor applications.

  • Hermanson, G. T. Bioconjugate Techniques, 3rd ed. Academic Press, 2013. Standard reference for protein and enzyme conjugation chemistries (amine-, thiol-, and click-based approaches).
  • Spicer, C. D.; Davis, B. G. Selectively modified proteins: methods and applications. Nature Communications 2014, 5, 4740. DOI: 10.1038/ncomms5740
  • Koniev, O.; Wagner, A. Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation. Chemical Society Reviews 2015, 44, 5495–5551. DOI: 10.1039/C5CS00051A
  • Diamandis, E. P.; Christopoulos, T. K. Immunoassay. Academic Press, 1996. Foundational text describing enzyme reporters (HRP, alkaline phosphatase) in analytical assays.
  • Tosi, L.; et al. Site-selective enzyme conjugation for biosensing applications. Analytical Chemistry 2018, 90, 1231–1240. DOI: 10.1021/acs.analchem.7b04573

Bio-Synthesis peptides and bioconjugates have been used in peer-reviewed biochemical and analytical studies; specific vendor attribution varies by publication.

Why Choose Bio-Synthesis

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