Hydrophobic Peptide Synthesis

Hydrophobic peptides are enriched in nonpolar residues or contain long nonpolar stretches that reduce aqueous solubility and promote aggregation during synthesis and purification.

A common cause is on‑resin aggregation and secondary structure formation, which reduces chain mobility and suppresses coupling efficiency—amplifying deletion/truncation impurities.

We select the simplest route that reliably meets targets. Manageable sequences may be completed by optimized SPPS, while aggregation‑prone targets benefit from strategic fragment breakpoints and ligation chemistry for better control and reproducibility.

Yes. We plan synthesis and purification with solubility in mind and can recommend handling approaches aligned to your downstream application.

Purity is method‑dependent and can be limited by chromatographic resolution and intrinsic heterogeneity. We recommend acceptance criteria based on application and provide HPLC/MS data to support interpretation.

When a continuous SPPS route is unlikely to meet targets, fragment synthesis plus ligation chemistry (e.g., native chemical ligation) can improve success probability and analytical control.

For very long or protein‑like hydrophobic targets, enzyme‑assisted (expression‑based) strategies may be proposed as an alternative route when appropriate. We recommend the best route after sequence review.

Timelines depend on complexity and route. Optimized SPPS projects often require several weeks; fragment assembly/ligation or enzyme‑assisted routes may require additional time for intermediate preparation, assembly, purification, and analytical verification.