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Chemotherapy Case Study

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Background: A main challenge in chemotherapy is the delivery of an effective dose of a given cytotoxic agent to the tumor site. Immunotoxins are protein-based drugs consist of a target-specific binding domain with a cytotoxic domain to eliminate target cells. Such compounds are potentially therapeutic against diseases such as cancer. The B-subunit of shiga toxin (STXB), which is nontoxic and possess low immunogenicity, accurately binds to the globotriaosylceramide (GB3/CD77), that is expressed in high amounts on a number of human tumors for example pancreatic, colon, and breast cancer cells. Therefore, this toxin can be applied to target GB3-positive human tumors. In this study, we evaluate a new antitumor candidate called DT-STXB chimeric …show more content…

Key words: In silico modeling, diphtheria toxin, shiga like toxin part B, Cancer Immunotherapy.

Introduction
The patients with cancer, who is treated by surgery, chemotherapy and radiotherapy, the recurrence usually happens and in many cases the tumor become metastatic(1, 2). For many years, the general therapy of cancer was based on the nonspecific treatments with cytotoxic substances to kill neoplastic cells. Yet, chemotherapy have some limitations, because it causes damage to natural tissues and therefore the toxic doses must be confined(3). Because of confined remedial index of cytotoxic drugs and the potential of cancer cells to develop resistance to these medications, it is essential to improve the novel instruments to target aggressive malignancies alone, or in combination with cytotoxic factors. Antitumor action of bacterial toxins have recognized in numerous studies. The conjugated compound of bacterial toxins and the ligandhas assumed to kill several kinds of tumor (4-8) . Thus in this study we have selected DT and STXB as an antitumor agent. Native diphtheria toxin (DT) is a 538-amino acid protein containing three domains. Subunit A is the enzymatically active domain, Subunit B has a hydrophobic domain at the N-terminal portion, and the C-terminal portion of subunit B is the receptor-binding

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