Identification of Structure-Linked Activity on Bioactive Peptides from Sea Cucumber (Stichopus japonicus): A Compressive In Silico/In Vitro Study.

IF 3.3 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Frontiers in bioscience (Landmark edition) Pub Date : 2024-10-23 DOI:10.31083/j.fbl2910368
Hyo-Geun Lee, D P Nagahawatta, Jun-Geon Je, Jae-Young Oh, H H A C K Jayawardhana, N M Liyanage, M J M S Kurera, Si-Hyeong Park, You-Jin Jeon, Won-Kyo Jung, Yu Ri Choe, Hyun-Soo Kim
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Abstract

Background: A sea cucumber (Stichopus japonicus) is an invertebrate rich in high-quality protein peptides that inhabits the coastal seas around East Asian countries. Such bioactive peptides can be utilized in targeted disease therapies and practical applications in the nutraceutical industry.

Methods: Bioactive peptides were isolated from Stichopus japonicus through ultrafiltration and Sephadex G-10 size exclusion chromatography. The low-molecular-weight fraction (ACSH-III) showed the highest hydroxyl radical scavenging and angiotensin-converting enzyme (ACE) inhibitory activities. Subsequent purification of ACSH-III resulted in four fractions, of which ACSH-III-F3 and ACSH-III-F4 exhibited significant bioactivity.

Results: Peptides identified in these fractions, including Phenylalanine-Proline-Threonine-Tyrosine (FPTY) and Tyrosine-Proline-Serine-Tyrosine-Proline-Serine (YPSYPS), were characterized using high-performance liquid chromatography (HPLC) and quadrupole time-of-flight mass spectrometry (QTOF-MS). FPTY demonstrated the most potent antioxidant and antihypertensive activities among these peptides, with IC50 values of 0.11 ± 0.01 mg/mL for hydroxyl radicals and 0.03 ± 0.01 mg/mL for ACE inhibition. Docking simulations revealed strong binding affinities of these peptides to the active site of the ACE, with FPTY displaying interactions similar to those of the synthetic inhibitor lisinopril.

Conclusions: These findings suggest that the identified peptides, particularly FPTY, have potential applications as natural antioxidants and functional foods.

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鉴定海参生物活性肽的结构关联活性:硅学/体外压缩研究。
背景:海参(日本刺参)是一种栖息于东亚国家近海的无脊椎动物,富含优质蛋白肽。这些生物活性肽可用于疾病的靶向治疗和营养保健品行业的实际应用:方法:通过超滤和 Sephadex G-10 尺寸排阻色谱法从日本栉水母中分离出生物活性肽。低分子量馏分(ACSH-III)显示出最高的羟基自由基清除活性和血管紧张素转换酶(ACE)抑制活性。随后对 ACSH-III 进行纯化,得到四个馏分,其中 ACSH-III-F3 和 ACSH-III-F4 具有显著的生物活性:结果:利用高效液相色谱法(HPLC)和四极飞行时间质谱法(QTOF-MS)对这些馏分中鉴定出的多肽(包括苯丙氨酸-脯氨酸-苏氨酸-酪氨酸(FPTY)和酪氨酸-脯氨酸-丝氨酸-酪氨酸-脯氨酸-丝氨酸(YPSYPS))进行了表征。在这些多肽中,FPTY 的抗氧化和抗高血压活性最强,其抑制羟自由基的 IC50 值为 0.11 ± 0.01 mg/mL,抑制 ACE 的 IC50 值为 0.03 ± 0.01 mg/mL。对接模拟显示,这些多肽与 ACE 活性位点的结合亲和力很强,其中 FPTY 与合成抑制剂赖诺普利的相互作用相似:这些发现表明,已鉴定的多肽,尤其是 FPTY,具有作为天然抗氧化剂和功能食品的潜在应用价值。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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