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The research aims to isolate a low-molecular-weight peptide with antioxidant properties from Argentine squid by-products and assess its effects on neural cell growth.

May 26, 2026Foods0 citationsOpen Access

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Isolationof PASN from Argentine Squid Carcass By-Products Enhances Proliferation and Repair of hACs and PC12 In Vitro via Antioxidant Activity

HYHaoze YangShanghai Ocean University TWTianming WangShanghai Ocean University YKYaqi KongShanghai Ocean University

Key Points

The research aims to isolate a low-molecular-weight peptide with antioxidant properties from Argentine squid by-products and assess its effects on neural cell growth.
Size-exclusion chromatography was utilized to isolate the peptide fraction from squid carcass by-products.
In vitro assays were conducted on rat adrenal pheochromocytoma (PC12) cells and human astrocyte (hACs) cells under corticosterone-induced oxidative stress.
Spectroscopic and thermogravimetric analyses characterized the properties of the isolated peptide.
PASN demonstrated significant protection against oxidative injury, restoring total superoxide dismutase activity to 69.46% in hACs and 66.40% in PC12 cells.
Cell viability improved markedly, with LDH leakage reduction of 38.31% in hACs and 31.17% in PC12 cells.
PASN enhanced BDNF expression by 35.23% in hACs and 12.50% in PC12, while GAD1/2 levels increased by 102.66% and 31.31%, respectively.

Abstract

Marine by-products represent a promising source of bioactive peptides. This study aimed to isolate and characterize a low-molecular-weight peptide fraction with antioxidant activity from Argentine shortfin squid carcass by-products, and to evaluate in vitro its cytocompatibility and protective effects against corticosterone (CORT)-induced oxidative injury in rat adrenal pheochromocytoma (PC12) cells and human astrocyte (hACs) cells. Argentine squid antioxidant peptide (PASN) was obtained by size-exclusion chromatography and fractionation-based screening. PASN exhibited the strongest overall free-radical-scavenging activity and consisted predominantly of components below 1 kDa (211.73–1013.48 Da). Spectroscopic analyses indicated that enzymatic hydrolysis transformed its structure from a rigid triple-helix conformation to a more flexible conformation dominated by β-turns (50.78%) and random coils (17.38%). In addition, thermogravimetric analysis confirmed its excellent thermal stability, with an onset decomposition temperature as high as 244.81 °C, supporting its potential applicability in high-temperature food-processing matrices. In vitro assays demonstrated that PASN exhibited high biocompatibility and promoted proliferation of both PC12 cells and hACs, while significantly improving cell viability under CORT challenge. PASN also reduced lactate dehydrogenase (LDH) leakage (hACs: 38.31%; PC12: 31.17%) in both cell models and restored total superoxide dismutase (T-SOD) activity (hACs: 69.46%, PC12: 66.40%). Immunofluorescence further revealed that PASN rescued the expression of brain-derived neurotrophic factor (BDNF) (hACs: 35.23%, PC12: 12.50%) and glutamate decarboxylase (GAD1/2) (hACs: 102.66%, PC12: 31.31%), key markers associated with synaptic plasticity and GABAergic sleep regulation. Collectively, PASN is a thermally stable squid-derived peptide fraction that exerts antioxidant and cytoprotective effects in neural cell models in vitro and represents a promising sustainable candidate for nutraceutical development.

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Isolationof PASN from Argentine Squid Carcass By-Products Enhances Proliferation and Repair of hACs and PC12 In Vitro via Antioxidant Activity

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