Evidence map›Paper›PMID 42012727›Full record

ArticleMarine biotechnology (New York, N.Y.)2026

Purification, Identification, and Functional Validation of Anti-Inflammatory Peptides from Protein Hydrolysates of Asian Seabass, Lates Calcarifer by-Product.

Hui-Chen Lin, Chung-Chih Tseng, Jia-Yu Lu, Hua-Yi Liang, Chun-Hung Liu

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Article in Marine biotechnology (New York, N.Y.), 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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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Hui-Chen Lin *Nutrition Room, Zuoying Armed Forces General Hospital, Kaohsiung, 813204, Taiwan.
Chung-Chih Tseng *Institute of Medical Technology, College of Medicine, National Sun Yat-sen University, Kaohsiung, 80424, Taiwan.
Jia-Yu Lu *Nutrition Room, Zuoying Armed Forces General Hospital, Kaohsiung, 813204, Taiwan.
Hua-Yi LiangDepartment of Aquaculture, National Pingtung University of Science and Technology, Pingtung, 912301, Taiwan.
Chun-Hung LiuDepartment of Aquaculture, National Pingtung University of Science and Technology, Pingtung, 912301, Taiwan. chliu@mail.npust.edu.tw.

Funding

National Science and Technology Council, Taiwan 113-2313-B-020-007-MY3Zuoying Armed Forces General Hospital, Taiwan ZYAFGH_A_115010
6 · The paper itself

Abstract

Fish processing by-products are increasingly recognized as sustainable raw materials for generating bioactive protein hydrolysates. In the present study, hydrolysates derived from Asian seabass (Lates calcarifer) by-products were produced and their anti-inflammatory potential was investigated in lipopolysaccharide (LPS)-activated RAW264.7 macrophages. The results showed that the hydrolysates were non-cytotoxic at concentrations up to 0.5 mg/mL and significantly reduced nitric oxide (NO) production. Fractionation by ultrafiltration indicated that the 10–30 kDa fraction possessed the greatest inhibitory effect on NO release. Further purification using gel filtration chromatography concentrated the activity in Fraction F2, which effectively suppressed NO generation, decreased the expression of pro-inflammatory cytokines (TNF-α, IL6, and IL1β), and regulated anti-inflammatory mediators. Peptide identification by LC–MS/MS combined with in silico prediction (PreAIP) yielded five peptides with high anti-inflammatory potential. Molecular docking with the TLR4/MD-2 complex (PDB: 2Z64) revealed that two peptides, LALDIEIATYR (LR-11) and LKLLLL (LL-6), exhibited favorable and stable binding interactions. Synthetic peptide assays further confirmed that both LR-11 and LL-6 significantly attenuated LPS-induced inflammatory responses, with LR-11 demonstrating stronger activity. In addition, structure-activity relationship evaluation of LR-11 analogs suggested that its biological function was closely associated with preservation of the original amino acid sequence and balanced physicochemical properties. Overall, these findings highlight Asian seabass by-products as a valuable and sustainable source of anti-inflammatory peptides and identify LR-11 as a promising candidate for future applications in nutraceutical and therapeutic development.

Indexed as

Anti-Inflammatory AgentsBassFish ProteinsPeptidesPerciformesProtein HydrolysatesAmino Acid SequenceAnimalsBioactive Peptides, DietaryCytokinesLipopolysaccharidesMacrophagesMiceMolecular Docking SimulationNitric OxideRAW 264.7 CellsAnti-Inflammatory AgentsBioactive Peptides, DietaryCytokinesFish ProteinsLipopolysaccharidesNitric OxidePeptidesProtein HydrolysatesAnti-inflammatory activityAsian seabass (Lates calcarifer) by-productsBioactive peptidesCytokine regulationNitric oxide inhibition

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.