文献类型：期刊文献

中文题名：基于表面等离子体共振技术筛选马氏珠母贝肉酶解产物中血管紧张素转换酶抑制肽

英文题名：Selection of Angiotensin I Converting Enzyme Inhibitory Peptides from Enzymatic Hydrolysate of Pinctada martensii Using Surface Plasmon Resonance

作者：夏小雨[1,2];温财兴[1];曹文红[1,2];秦小明[1,2];李钰金[3];林海生[1,2];陈忠琴[1,2];郑惠娜[1,2];朱国萍[1,2];高加龙[1,2]

机构：[1]广东海洋大学食品科技学院,广东湛江524088;[2]国家贝类加工技术研发分中心(湛江),广东省水产品加工与安全重点实验室,广东省海洋生物制品工程实验室,水产品深加工广东普通高校重点实验室,广东湛江524088;[3]中国海洋大学食品科学与工程学院,山东青岛266003

年份：2025

卷号：46

期号：7

起止页码：143

中文期刊名：食品科学

外文期刊名：Food Science

收录：北大核心2023、、EI(收录号：20251418181696)、北大核心

基金：贝类产业技术体系项目(CARS-49);湛江市科技计划项目(230906164548720);山东省重点扶持区域紧缺人才项目(鲁发改动能办[2024]658号)。

语种：中文

中文关键词：马氏珠母贝;血管紧张素转换酶抑制肽;表面等离子体共振;酶抑制动力学;分子对接

外文关键词：Pinctada martensii;angiotensin I converting enzyme inhibitory peptide;surface plasmon resonance;enzymatic inhibition kinetics;molecular docking

中文摘要：本研究采用表面等离子体共振技术,以血管紧张素转换酶(angiotensin I converting enzyme,ACE)为蛋白配体,分析马氏珠母贝肉蛋白酶解产物(protein hydrolysate of Pinctada martensii,PHPM)超滤组分与配体的结合情况,利用质谱鉴定结合肽段的氨基酸序列后,筛选潜在抑制ACE活性强的肽段进行合成,研究其体外ACE抑制活性、抑制类型及多肽与ACE蛋白的相互作用。结果显示,PHPM分子质量在3 000~5 000 Da的超滤组分与ACE蛋白具有较强的结合信号,在结合物质的肽序列中优选出4种具有潜在活性的ACE抑制肽进行合成,其中多肽SLPWPMKPMNLIE的半数抑制浓度最低,并且通过氢键与ACE蛋白C端结构域的疏水口袋结合。

外文摘要：Surface plasmon resonance(SPR)technology was used to analyze the binding of the three ultrafiltration fractions of the protein hydrolysate of Pinctada martensii(PHPM)with angiotensin I converting enzyme(ACE)as a protein ligand.The amino acid sequences of the bound peptides were identified by mass spectrometry(MS)and those with strong inhibitory potential against ACE were selected and synthesized.The in vitro ACE inhibitory activity and inhibition type of the peptides were studied as well as their interaction with ACE.It was found that the ultrafiltration fraction with a molecular mass of 3000–5000 Da had a strong binding signal to ACE.Among the four synthesized ACE inhibitory peptides,SLPWPMKPMNLIE had the lowest 50%inhibitory concentration(IC50)value and bound to the hydrophobic pocket of the C domain in ACE through hydrogen bonding.