ArticleFrontiers in bioengineering and biotechnology2026
Engineering small peptide secretion in
Article in Frontiers in bioengineering and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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11 authors.
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Abstract
Background: Small peptides have emerged as an important class of biologics with broad therapeutic applications. Limitations of conventional solid-phase synthesis have intensified the interest in microbial production systems. Methods: To systematically investigate bottlenecks in small peptide secretion, we established the 3×FLAG peptide (23 amino acids) as a tractable, immunologically detectable model system. We evaluated the impact of peptide chain length and signal sequence selection on secretory performance. Furthermore, we assessed the effect of overexpressing the translocon components and conducted a random mutagenesis screen to identify novel genetic determinants influencing secretion. Finally, we tested the transferability of our engineering strategies on the disulfide-rich peptide dQ-brazzein and the therapeutic fusion peptides α-melanocyte-stimulating hormone and salmon calcitonin. Results: Secretion efficiency exhibited a strong dependency on peptide chain length and signal sequence selection, likely reflecting limitations during endoplasmic reticulum translocation. Overexpression of Sec61 partially alleviated this bottleneck, enhancing secretion approximately 2-fold. Through the random mutagenesis screen, we identified Conclusion: This study provides a systematic evaluation of engineering strategies targeting the unique constraints of very small (<3.5 kDa) peptide secretion in
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