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Biomedical subjects

Minghui Yu

Publications and source records attributed to Minghui Yu.

5 recordsLinked to original sources

Quadruplex-to-duplex transition of G-rich oligonucleotides probed by cationic water-soluble conjugated polyelectrolytes.

G-quartet DNA converts to duplex form in the presence of its complementary strand. This conformational change can be detected in real time by a homogeneous assay method based on the signal amplification of conjugated polyelectrolytes and the specific interaction of intercalating dyes with double-stranded DNA (dsDNA). The probe solution contains a cationic, conjugated polymer (CCP), G-quadruplex labeled with a fluorescein at the 5'-terminus (G-quadruplex-Fl), and ethidium bromide (EB). The addition of a complementary target results in the transition from G-quadruplex to duplex (dsDNA-Fl) and EB intercalation within the duplex structure. Excitation of the CCP leads to energy transfer from CCP to dsDNA-Fl (FRET-1) and then energy transfer from dsDNA-Fl to EB (FRET-2). Increasing the number of mismatched bases discourages dsDNA formation, which is detected in the assay.

Cations↗

A novel method based on ligase detection reaction for low abundant YIDD mutants detection in hepatitis B virus.

A novel method based on ligase detection reaction (LDR) coupled with polymerase chain reaction (PCR) was used in this study to detect low abundant YIDD mutants in hepatitis B virus (HBV), which was able to detect 10(2) mutants from 10(8) wild type copies in plasmids and 10(3) from 10(7) in clinical serum samples. Direct sequencing and microarray hybridization were selected for sensitivity comparison together with this assay. By direct sequencing, 6 of 50 clinical specimens infected with HBV were found to be YIDD and the others to be YMDD, while by microarray hybridization, 28 specimens were detected to contain both YMDD and YIDD, and the others contained YMDD only, and with this assay, 31 specimens containing both YMDD and YIDD were detected with the others containing YMDD only, which indicated that the assay was relatively more sensitive.

Journal Article↗

Selection and identification of human gonadotropin-releasing hormone promoter binding peptides by phage display-CEMSA.

Specific interactions between transcription factors and cis-acting DNA sequences form the molecular basis of gene expression regulation. Here, we applied phage display technology to DNA-protein interaction studies. A phage-displayed peptide library was used to select Gonadotropin-releasing hormone promoter (GP) binding peptides. After four sequential rounds of biopanning on GP-conjugated magnetic beads, phage clones encoding GQPTPRNAGLPL (B6), SRLNVEPLTTYS (B3), and TTLHWASLTTGR (B11) were enriched. Phages bearing these peptides showed specific binding to GP in solution by capillary electrophoresis mobility shift assay (CEMSA). In addition, some human transcription factors were speculated as the potential transcription factors or co-activators of GnRH gene by bioinformatic analysis. These results suggest that phage display-CEMSA methodology should be a powerful tool to screen and identify site-specific DNA-binding peptides.

Amino Acid Sequence↗