Identification of an antibody fragment specific for androgen-dependent prostate cancer cells

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• 作者：Ryan M Williams (1) (2)
  Cyrus J Hajiran (3)
  Sara Nayeem (1)
  Letha J Sooter (1)
  
  1. Department of Basic Pharmaceutical Sciences ; West Virginia University ; 1 Medical Center Drive ; PO Box 9530 ; Morgantown ; WV ; 26506 ; USA
  2. Memorial Sloan Kettering Cancer Center ; Molecular Pharmacology & Chemistry Program ; 1275 York Ave. ; New York ; NY ; 10065 ; USA
  3. Department of Biology ; West Virginia University ; 53 Campus Drive ; PO Box 6057 ; Morgantown ; WV ; 26506 ; USA
  
• 关键词：Prostate cancer ; Antibody fragment ; scFv ; Library screening ; Yeast
• 刊名：BMC Biotechnology
• 出版年：2014
• 出版时间：December 2014
• 年：2014
• 卷：14
• 期：1
• 全文大小：880 KB
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• 刊物类别：Chemistry and Materials Science
• 刊物主题：Biotechnology
  Life Sciences
  Plant Breeding/Biotechnology
  Stem Cells
  Transgenics
  
• 出版者：BioMed Central
• ISSN：1472-6750

文摘

Background Prostate cancer is the most-diagnosed non-skin cancer among males in the US, and the second leading cause of cancer-related death. Current methods of treatment and diagnosis are not specific for the disease. This work identified an antibody fragment that binds selectively to a molecule on the surface of androgen-dependent prostate cancer cells but not benign prostatic cells. Results Antibody fragment identification was achieved using a library screening and enrichment strategy. A library of 109 yeast-displayed human non-immune antibody fragments was enriched for those that bind to androgen-dependent prostate cancer cells, but not to benign prostatic cells or purified prostate-specific membrane antigen (PSMA). Seven rounds of panning and fluorescence-activated cell sorting (FACS) screening yielded one antibody fragment identified from the enriched library. This molecule, termed HiR7.8, has a low-nanomolar equilibrium dissociation constant (Kd) and high specificity for androgen-dependent prostate cancer cells. Conclusions Antibody fragment screening from a yeast-displayed library has yielded one molecule with high affinity and specificity. With further pre-clinical development, it is hoped that the antibody fragment identified using this screening strategy will be useful in the specific detection of prostate cancer and in targeted delivery of therapeutic agents for increased efficacy and reduced side effects.