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Nanocarriers as an Emerging Platform for Cancer Therapy
Published in Lajos P. Balogh, Nano-Enabled Medical Applications, 2020
Dan Peer, Jeffrey M. Karp, Seungpyo Hong, Omid C. Farokhzad, Rimona Margalit, Robert Langer
Although using genomics and proteomics technology to choose appropriate targets is an active area of research, to date no clinically effective targets have been identified. Creating new technologies to enhance selectivity and targeting efficacy with existing targets seem more promising. For example, fusion proteins can be created by combining two or more genes to produce a new protein with desired properties. Antibodies can be engineered so they bind to their target with high affinity, and using molecular biology techniques, it is possible to design protein-based ligand mimetics based on the structure of a receptor. Dimerization of proteins or peptides can increase ligand affinity through divalency—two simultaneous binding events, usually involving concurrent binding of a protein or a peptide to the two Fc domains of an antibody (Fig. 2.2b). For example, dimerization of a low-affinity scFv (also known as diabody) against the ErbB2, led to enhanced tumour localization in a mouse tumour model [37].
Enzyme Catalysis
Published in Harvey W. Blanch, Douglas S. Clark, Biochemical Engineering, 1997
Harvey W. Blanch, Douglas S. Clark
Fusion proteins can also be constructed to simplify purification. One approach is to select a bacterial sequence that codes for a polypeptide that can be isolated by affinity chromatography (Section 6.4.2). An alternative is to fuse a synthetic gene sequence coding for polyarginine to the eukaryotic gene of interest. Cation-exchange chromatography can then be used to purify the positively charged recombinant fusion protein. In any event, the following points should be kept in mind when designing a genetic construction for purification purposes:
Nanoinformatics: An Emerging Trend in Cancer Therapeutics
Published in Rajesh Singh Tomar, Anurag Jyoti, Shuchi Kaushik, Nanobiotechnology, 2020
Medha Pandya, Snehal Jani, Vishakha Dave, Rakesh Rawal
The genes originally code for separate proteins. The fusion proteins or chimeric proteins formulate through the joining of two or more genes that generate a fusion gene or oncogene. Translation of this fusion gene results in a single polypeptide with functional properties derived from each of the original proteins. Chimeric proteins occur naturally when a large-scale mutation or chromosomal translocation produces a novel coding sequence containing components of the coding sequences from two different genes. Naturally, occurring fusion proteins are important in cancer, where they may function as oncoproteins. The fusion gene can be transcribed, spliced, and translated to produce a functional fusion protein. Many important cancer-promoting oncogenes are fusion genes produced in this way. For instance, the AF9 gene from chromosome 9 joints with the MLL gene on chromosome 11, to form MLL-AF9 fusion gene (Figure 11.3). Amongst all MLL translocations, around 50% of infant AML cases comprises of t (9, 11) (p22, q23) rearrangement. AF9 gene, also known as LTG9 or MLLT3, is located at short arm p22 of chromosome 9 [30, 43, 61]. The accumulating evidence suggests that leukemogenesis caused by the formation of the MLL-AF9 fusion protein through the mechanism of these partner genes is unsigned. In contrast, few in-vitro and in-vivo examination revealed that MLL-AF9 alters myeloid progenitor cells and suppresses specific HOX genes. The mice with knock-in MLL-AF9 fusion genes demonstrated the abnormal proliferation of hematopoietic cells and developed AML identical to the patient with t (9; 11) translocation [12, 20, 31]. Additional to this, MLL, and AF9 wild protein participates indispensably during the hematopoiesis/embryogenesis process and are elements of protein complexes resulting in target gene transcriptional initiation (MLL) and elongation (AF9).
Cloning, expression and characterization of a HER2-alpha luffin fusion protein in Escherichia coli
Published in Preparative Biochemistry and Biotechnology, 2019
Farzaneh Barkhordari, Nooshin Sohrabi, Fatemeh Davami, Fereidoun Mahboudi, Yeganeh Talebkhan Garoosi
Ribosome-Inactivating Proteins (RIPs) (26–31 kDa) can prevent protein synthesis through depurination of the large ribosomal RNA (rRNA) and ribosome blockage.[17] They are generally derived from plants, bacteria and fungi and considered as antibacterial, antifungal and anti-viral agents with a variety of antitumor, immunosuppressive and antifertility activities.[17–19] The most studied plant toxins include ricin, abrin, saporin, Bryodin-L, gelonin, and luffin.[20] Although plant toxins have highly efficient cell-killing characteristics but they lack selectivity in targeting cells. By conjugation of RIP proteins to the antibodies or hormones, the constructed fusion proteins can represent toxicity toward specific cell types.[21,22] In a previous study, hIL-2-Luffin P1 immunotoxin has shown strong effects on inhibition of T cell proliferation representing promising efficiency in the treatment of autoimmune diseases.[23] Alpha luffin is the smallest RIP molecule (27 kDa) which has been identified and isolated from the seeds of Luffa cylindrical.[24] Many studies have shown that α-luffin inhibited the proliferation of cancer cell lines.[25] In an attempt, the conjugation of α-luffin to monoclonal antibodies against human melanoma cells exhibited in vitro growth inhibition.[26]