| Literature DB >> 16027006 |
Hui Wang1, Zhen Yan, Jihong Shi, Wei Han, Yingqi Zhang.
Abstract
The tumor vasculature is a suitable target for cancer treatment. RGD-4C (CDCRGDCFC) peptide can bind to human alphav integrins, which are known to be selectively expressed in human tumor blood vessels. Some studies showed that coupling anticancer drugs or peptides to the RGD peptides yielded compounds with increased efficacy against tumors and lowered toxicity to normal tissues in mice. TNF-alpha mutant (rmhTNF-alpha) that we previously constructed has been proved to have stronger antitumor effect compared with TNF-alpha. To increase antitumor effect and lower toxicity of rmhTNF-alpha, we coupled RGD4C to the N-terminal of rmhTNF-alpha (termed RGD4C-rmhTNF) and expressed RGD4C-rmhTNF in Escherichia coli. Here, we describe the expression, purification, and characterization of RGD4C-rmhTNF.Entities:
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Year: 2005 PMID： 16027006 DOI： 10.1016/j.pep.2005.05.009
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650