Amine‑selective side‑chain functionalization for controlled lysine labeling, peptide conjugation, and distribution‑aware analytics—designed, executed, and verified by Bio‑Synthesis.
Lysine‑selective peptide chemistry targets primary amines—most importantly the lysine ε‑amine—to install labels, linkers, or payloads. Because many peptides contain multiple lysines (and a reactive N‑terminus), amine‑reactive chemistry often produces a degree‑of‑labeling (DoL) distribution rather than a single site. At Bio‑Synthesis, we control heterogeneity with stoichiometry and condition design, or we enforce site‑defined lysine using sequence/strategy when strict specificity is required.
Overview schematic: lysine labeling is amine‑reactive—control DoL with equivalents/pH/buffer, or design a single reactive amine for site-defined outcomes.
If strict site‑specificity is required, engineer a single reactive amine (single Lys or orthogonal amino handle) and minimize competing amines (e.g., N‑terminus) via design/protection. If distributions are acceptable, we tune equivalents, pH, and buffer to hit your DoL target and verify by analytics.
Related: Cysteine‑selective chemistry, Side‑chain functionalization, Click chemistry peptides.
Amine‑reactive dyes, biotin tags, and linkers are widely available and well‑characterized.
No thiol oxidation control required; workflows are straightforward for many labeling applications.
You can tune degree‑of‑labeling (single label vs distribution) by equivalents, pH, and time.
Useful when the exact attachment site is less important than signal, capture, or overall label density.
Multiple Lys residues and the N‑terminus can yield statistical mixtures unless design enforces a single reactive amine.
We verify outcomes with analytical HPLC/UPLC and LC–MS (when feasible), aligned to your DoL target.
“Lysine‑selective” typically means amine‑reactive labeling. Choose chemistry based on DoL control, buffer compatibility, and whether you need a distribution outcome or a site‑defined attachment.
Tell us your target DoL, buffer, and whether N‑terminal labeling is acceptable—we’ll recommend the lowest‑risk route and QC plan.
Most “lysine‑selective” labeling is statistical unless the sequence/strategy enforces a unique site.
We align reaction conditions and acceptance criteria to your application (screening vs functional conjugate vs immobilization).
Want lysine labeling? Decide whether distributions are acceptable → set DoL target → avoid amine buffers → verify by HPLC/LC–MS (when feasible); for strict single‑site conjugation, enforce one reactive amine or use cysteine.
The N‑terminal α‑amine can compete with lysine ε‑amines depending on pH and local environment.
Primary amine buffers (e.g., Tris) compete with NHS esters. We recommend amine‑free buffers.
Higher pH increases amine reactivity but also hydrolysis of activated esters; conditions must be tuned.
Multiple amines produce mixtures. Decide up front: single label, defined DoL distribution, or site‑defined strategy.
Hydrophobic peptides can limit effective labeling. We can recommend solubilizing tactics consistent with your chemistry.
We confirm conversion/purity by HPLC/UPLC and assess DoL by LC–MS (when feasible), aligned to your acceptance criteria.
For lysine labeling, the key deliverable is often degree‑of‑labeling confirmation (single label vs distribution). We align QC to your goal rather than forcing a one‑size‑fits‑all metric.
Lysine-selective peptide chemistry targets primary amines—most importantly the ε‑amine on lysine side chains—to install labels, linkers, or payloads. Because many peptides contain multiple lysines (and a reactive N‑terminus), lysine chemistry often produces a degree‑of‑labeling distribution unless the sequence or protection strategy enforces a single reactive amine.
Choose lysine chemistry when partial labeling is acceptable, when lysine placement is functionally convenient, or when thiol handling is undesirable. If you need strict single‑site conjugation, a single engineered cysteine (or an orthogonal handle) is often lower risk.
We control DoL by reagent equivalents, pH window, buffer selection, reaction time, and quench strategy. For multi‑lysine sequences we set expectations up front (single label vs distribution) and align purification/QC to the intended outcome.
Yes. The N‑terminal α‑amine frequently competes with lysine ε‑amines depending on pH and local environment. If N‑terminal labeling is undesirable, we can recommend sequence design or protection/capping options to bias toward lysine.
Primary amine buffers (e.g., Tris) compete with NHS esters and can reduce yield. We recommend amine-free buffers and conditions tailored to your payload and peptide solubility.
We use analytical HPLC/UPLC and LC–MS (when feasible) to confirm mass shifts and assess product distributions. For heterogeneous labeling outcomes, we report distribution-aware analytics consistent with the DoL target.
For the fastest quote, send your sequence(s), lysine count/positions, desired chemistry (or “recommend”), payload/handle details, buffer context, and purity/quantity targets. We’ll recommend practical specifications and a synthesis/QC plan aligned to your goal.
Key references on amine-reactive labeling, bioconjugation selectivity, and practical considerations for controlling degree of labeling and heterogeneity in lysine modification workflows.
Want lysine modification references tailored to your payload class (fluorophores, biotin, linkers) or to achieve a specific DoL target? Tell us your use case and we’ll tailor the plan.
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