Alocasia macrorrhiza rhizome lectin inhibits growth of pathogenic bacteria and human lung cancer cell in vitro and Ehrlich ascites carcinoma cell in vivo in mice

IF 1.4 4区生物学 Q4 BIOCHEMICAL RESEARCH METHODS

Protein expression and purification Pub Date : 2024-04-16 DOI:10.1016/j.pep.2024.106484

Hossain Mohammad Hridoy , Md Pervez Hossain , Md Hasan Ali , Imtiaj Hasan , Md Belal Uddin , Mohammad Taufiq Alam , Syed Rashel Kabir

{"title":"Alocasia macrorrhiza rhizome lectin inhibits growth of pathogenic bacteria and human lung cancer cell in vitro and Ehrlich ascites carcinoma cell in vivo in mice","authors":"Hossain Mohammad Hridoy , Md Pervez Hossain , Md Hasan Ali , Imtiaj Hasan , Md Belal Uddin , Mohammad Taufiq Alam , Syed Rashel Kabir","doi":"10.1016/j.pep.2024.106484","DOIUrl":null,"url":null,"abstract":"<div>Cancer and antibiotic resistance represent significant global challenges, affecting public health and healthcare systems worldwide. Lectin, a carbohydrate-binding protein, displays various biological properties, including antimicrobial and anticancer activities. This study focused on anticancer and antibacterial properties of Alocasia macrorrhiza lectin (AML). AML, with a molecular weight of 11.0 ± 1.0 kDa was purified using Ion-exchange chromatography, and the homotetrameric form was detected by gel-filtration chromatography. It agglutinates mouse erythrocytes, that was inhibited by 4-Nitrophenyl-α-d-mannopyranoside. Maximum hemagglutination activity was observed below 60 °C and within a pH range from 8 to 11. Additionally, it exhibited moderate toxicity against brine shrimp nauplii with LD50 values of 321 μg/ml and showed antibacterial activity against Escherichia coli and Shigella dysenteriae. In vitro experiments demonstrated that AML suppressed the proliferation of mice Ehrlich ascites carcinoma (EAC) cells by 35 % and human lung cancer (A549) cells by 40 % at 512 μg/ml concentration. In vivo experiments involved intraperitoneal injection of AML in EAC-bearing mice for five consecutive days at doses of 2.5 and 5.0 mg/kg/day, and the results indicated that AML inhibited EAC cell growth by 37 % and 54 %, respectively. Finally, it can be concluded that AML can be used for further anticancer and antibacterial studies.</div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"219 ","pages":"Article 106484"},"PeriodicalIF":1.4000,"publicationDate":"2024-04-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein expression and purification","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1046592824000561","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}

引用次数: 0

Abstract

Cancer and antibiotic resistance represent significant global challenges, affecting public health and healthcare systems worldwide. Lectin, a carbohydrate-binding protein, displays various biological properties, including antimicrobial and anticancer activities. This study focused on anticancer and antibacterial properties of Alocasia macrorrhiza lectin (AML). AML, with a molecular weight of 11.0 ± 1.0 kDa was purified using Ion-exchange chromatography, and the homotetrameric form was detected by gel-filtration chromatography. It agglutinates mouse erythrocytes, that was inhibited by 4-Nitrophenyl-α-d-mannopyranoside. Maximum hemagglutination activity was observed below 60 °C and within a pH range from 8 to 11. Additionally, it exhibited moderate toxicity against brine shrimp nauplii with LD₅₀ values of 321 μg/ml and showed antibacterial activity against Escherichia coli and Shigella dysenteriae. In vitro experiments demonstrated that AML suppressed the proliferation of mice Ehrlich ascites carcinoma (EAC) cells by 35 % and human lung cancer (A549) cells by 40 % at 512 μg/ml concentration. In vivo experiments involved intraperitoneal injection of AML in EAC-bearing mice for five consecutive days at doses of 2.5 and 5.0 mg/kg/day, and the results indicated that AML inhibited EAC cell growth by 37 % and 54 %, respectively. Finally, it can be concluded that AML can be used for further anticancer and antibacterial studies.

查看原文本刊更多论文

大根藻根茎凝集素可抑制致病菌、体外人类肺癌细胞和体内小鼠艾氏腹水癌细胞的生长

癌症和抗生素耐药性是全球性的重大挑战，影响着全世界的公共卫生和医疗保健系统。凝集素是一种碳水化合物结合蛋白，具有多种生物特性，包括抗菌和抗癌活性。这项研究的重点是大叶女贞凝集素（AML）的抗癌和抗菌特性。采用离子交换色谱法纯化了分子量为 11.0 ± 1.0 kDa 的大根木通凝集素，并通过凝胶过滤色谱法检测了其同型四聚体形式。它能凝集小鼠红细胞，并受 4-硝基苯基-α-d-吡喃甘露糖苷的抑制。在温度低于 60 °C 和 pH 值介于 8 到 11 之间时，血凝活性最高。此外，它对盐水虾稚虫具有中等毒性，半数致死剂量为 321 μg/ml，并对大肠杆菌和志贺痢疾杆菌具有抗菌活性。体外实验表明，在 512 μg/ml 浓度下，AML 可抑制小鼠艾氏腹水癌（EAC）细胞增殖 35%，人肺癌（A549）细胞增殖 40%。体内实验是以 2.5 毫克/千克/天和 5.0 毫克/千克/天的剂量连续五天给 EAC 小鼠腹腔注射 AML，结果表明 AML 对 EAC 细胞生长的抑制率分别为 37% 和 54%。最后，可以得出结论，AML 可用于进一步的抗癌和抗菌研究。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Protein expression and purification 生物-生化研究方法

CiteScore

3.70

自引率

6.20%

发文量

120

审稿时长

32 days

期刊介绍： Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.