Abstract | OBJECTIVE: RESULTS: A 12-mer phage peptide library was screened against immobilized CD44 protein. Bound phage counts using ELISA were performed to identify phage clones carrying the most highly selective peptide, which termed RP-1. Immunofluorescence and flow cytometry analysis indicated that the consensus peptide RP-1 could bind to CD44-positive gastric cancer cells with mean fluorescence intensities significantly higher than that of CD44-negative cells. CD44 knockdown led to decreased binding activity of RP-1 to the same cell line. Tissue array technique was used to identify the relationship (r = 0.556) between peptide binding and CD44 detection on gastric cancer tissues. Further, the hyaluronan-binding domain of CD44 was docked with RP-1 using computer modeling/docking approaches, revealing a RP-1/CD44 interaction with geometrical and energy match (-8.6 kcal/mol). CONCLUSIONS: The RP-1 peptide we screened exhibits affinity and specificity to CD44 on cells and has the potential to be used as a candidate probe for gastric cancer cell targeting.
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Authors | Dan Zhang, Huan Jia, Yan Wang, Wei-Ming Li, Ying-Chun Hou, Shi-Wei Yin, Thomas D Wang, Shui-Xiang He, Shao-Ying Lu |
Journal | Biotechnology letters
(Biotechnol Lett)
Vol. 37
Issue 11
Pg. 2311-20
(Nov 2015)
ISSN: 1573-6776 [Electronic] Netherlands |
PMID | 26140900
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- CD44 protein, human
- Hyaluronan Receptors
- Peptide Library
- Peptides
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Topics |
- Cell Line, Tumor
- Humans
- Hyaluronan Receptors
(chemistry, metabolism)
- Immunohistochemistry
- Molecular Docking Simulation
- Peptide Library
- Peptides
(chemistry, genetics, metabolism)
- Stomach Neoplasms
(chemistry, metabolism)
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