Antitumor and Cytotoxic Protein Component from Aporrectodea longa: Purification, and Characterization Studies

Background: Cancer, a metabolic disorder with multifactorial input, is the most complex human disease to study and find a cure. Over several decades, massive research effort leads to a better understanding molecular biology of cancer and its progression. Plants and animals both were explored for novel anti-tumor agents, and enzyme-based drugs have shown significant results. These animals evolved with an enzyme with promiscuous nature capable of catalyzing multiple biochemical reactions. Enzymes are an integral part of animal physiology and are reported excellent sources of the drug. Objectives: The study aimed to isolate, purify and characterize the protein component from Aporrectodea longa for anti-cancer potential. Materials and Methods: A. longa species earthworms were collected and processed for the extraction of total protein content. The anti-tumor protein component was purified via salt precipitation, charge-based purification, and sizebased purification. SDS-PAGE was used to investigate molecular weight information. The anti-tumor activity was evaluated using different cell lines, including MCF 7, Hep G2, and HT 29 with Cisplatin, 5-fluorouracil, and tamoxifen as a standard anti-cancer drug. Results: The isolated and purified protein fraction had shown proteolytic activity against casein and fibrinogen. Protein fraction represents a serine protease and average molecular weight of nearly 42kDa. The result shows protein component possesses excellent antitumor activity analyzed by MTT assay. Conclusion: Anti-tumor activity of isolated and purified protein fraction from A. longa may serve as a potential candidate for anti-cancer therapy. However, molecular studies are required to explore the precise mechanism of action of candidate protein.