{"title":"新型核桃粕弹性酶抑制肽的制备、鉴定及分子对接","authors":"Yu Xiong , Peng Peng , Shi-Jia Chen, Min Chang, Qian Wang, Sheng-Nan Yin, Di-Feng Ren","doi":"10.1016/j.fochms.2022.100139","DOIUrl":null,"url":null,"abstract":"<div><p>This study aimed to isolate bioactive peptides with elastase inhibitory activity from walnut meal via ultrasonic enzymatic hydrolysis. The optimal hydrolysis conditions of walnut meal protein hydrolysates (WMPHs) were obtained by response surface methodology (RSM), while a molecular weight of<3 kDa fraction was analyzed by LC-MS/MS, and 556 peptides were identified. PyRx virtual screening and Autodock Vina molecular docking revealed that the pentapeptide Phe-Phe-Val-Pro-Phe (FFVPF) could interact with elastase primarily through hydrophobic interactions, hydrogen bonds, and π-sulfur bonds, with a binding energy of −5.22 kcal/mol. The verification results of inhibitory activity showed that FFVPF had better elastase inhibitory activity, with IC<sub>50</sub> values of 0.469 ± 0.01 mg/mL. Furthermore, FFVPF exhibited specific stability in the gastric environment. These findings suggest that the pentapeptide FFVPF from defatted walnut meal could serve as a potential source of elastase inhibitors in the food, medical, and cosmetics industries.</p></div>","PeriodicalId":34477,"journal":{"name":"Food Chemistry Molecular Sciences","volume":"5 ","pages":"Article 100139"},"PeriodicalIF":4.1000,"publicationDate":"2022-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2666566222000673/pdfft?md5=c536873f31bc3cb9ad8d37f807cd3c34&pid=1-s2.0-S2666566222000673-main.pdf","citationCount":"2","resultStr":"{\"title\":\"Preparation, identification, and molecular docking of novel elastase inhibitory peptide from walnut (Juglans regia L.) meal\",\"authors\":\"Yu Xiong , Peng Peng , Shi-Jia Chen, Min Chang, Qian Wang, Sheng-Nan Yin, Di-Feng Ren\",\"doi\":\"10.1016/j.fochms.2022.100139\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>This study aimed to isolate bioactive peptides with elastase inhibitory activity from walnut meal via ultrasonic enzymatic hydrolysis. The optimal hydrolysis conditions of walnut meal protein hydrolysates (WMPHs) were obtained by response surface methodology (RSM), while a molecular weight of<3 kDa fraction was analyzed by LC-MS/MS, and 556 peptides were identified. PyRx virtual screening and Autodock Vina molecular docking revealed that the pentapeptide Phe-Phe-Val-Pro-Phe (FFVPF) could interact with elastase primarily through hydrophobic interactions, hydrogen bonds, and π-sulfur bonds, with a binding energy of −5.22 kcal/mol. The verification results of inhibitory activity showed that FFVPF had better elastase inhibitory activity, with IC<sub>50</sub> values of 0.469 ± 0.01 mg/mL. Furthermore, FFVPF exhibited specific stability in the gastric environment. These findings suggest that the pentapeptide FFVPF from defatted walnut meal could serve as a potential source of elastase inhibitors in the food, medical, and cosmetics industries.</p></div>\",\"PeriodicalId\":34477,\"journal\":{\"name\":\"Food Chemistry Molecular Sciences\",\"volume\":\"5 \",\"pages\":\"Article 100139\"},\"PeriodicalIF\":4.1000,\"publicationDate\":\"2022-12-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S2666566222000673/pdfft?md5=c536873f31bc3cb9ad8d37f807cd3c34&pid=1-s2.0-S2666566222000673-main.pdf\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry Molecular Sciences\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2666566222000673\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry Molecular Sciences","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2666566222000673","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Preparation, identification, and molecular docking of novel elastase inhibitory peptide from walnut (Juglans regia L.) meal
This study aimed to isolate bioactive peptides with elastase inhibitory activity from walnut meal via ultrasonic enzymatic hydrolysis. The optimal hydrolysis conditions of walnut meal protein hydrolysates (WMPHs) were obtained by response surface methodology (RSM), while a molecular weight of<3 kDa fraction was analyzed by LC-MS/MS, and 556 peptides were identified. PyRx virtual screening and Autodock Vina molecular docking revealed that the pentapeptide Phe-Phe-Val-Pro-Phe (FFVPF) could interact with elastase primarily through hydrophobic interactions, hydrogen bonds, and π-sulfur bonds, with a binding energy of −5.22 kcal/mol. The verification results of inhibitory activity showed that FFVPF had better elastase inhibitory activity, with IC50 values of 0.469 ± 0.01 mg/mL. Furthermore, FFVPF exhibited specific stability in the gastric environment. These findings suggest that the pentapeptide FFVPF from defatted walnut meal could serve as a potential source of elastase inhibitors in the food, medical, and cosmetics industries.