Hsien-Yu Tsai - Academia.edu (original) (raw)
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Papers by Hsien-Yu Tsai
Hepatitis B virus (HBV) X protein (HBx) plays a key role in the development of hepatocellular car... more Hepatitis B virus (HBV) X protein (HBx) plays a key role in the development of hepatocellular carcinoma (HCC) in HBV carriers. A drug that can bind to the promoter region of HBV may shut down the expression of HBx and subsequently prevent the development of HCC in the HBV carrier. We have constructed a seven amino acid residue peptide library on a TentaGel resin using a combinatorial one-bead one-sequence peptide synthesis method. The fluorescently labeled eicosanucleotide (5¢-(6-FAM) CTTTTGGGCT TTGCTGCCCC-3¢) of the HBx promoter region was used as a monitor to screen for peptides that have high binding affinity to the HBx promoter. Two heptapeptides, KAPLFSI and SRVRMTW, were identified, and synthesized. The binding affinities of the peptides to the HBx promoter oligonucleotide were determined using Surface Plasmon Resonance (SPR). The peptide KAPLFSI had a greater binding affinity constant (k a ) and equilibrium constant (K D ) than SRVRMTW. The k a and K D values with the full X-promoter sequence were found to be 1.425 E+5 (1/Ms) and 1.186 E-8 (M), respectively. The peptide may open a new route for tumor suppression in HBV carriers. . Biacore Sensorgrams of the interactions between the peptide sequence KAPLFSI and the X-promoter oligonucleotide sequences at different concentrations.
Glycosylation is a common protein modification that is of interest in current cancer research bec... more Glycosylation is a common protein modification that is of interest in current cancer research because altered carbohydrate moieties are often found during cancer progress. A search for biomarkers in human lung cancer serum samples using glycoproteomic approaches identified fucosylated haptoglobin (Hp) significantly increased in serum of each subtype of lung cancer compared to normal donors. In addition, MS provided evidence of an increase of Hp fucosylation; the glycan structure was determined to be an a 2,6-linked tri-sialylated triantennary glycan containing a1,3-linked fucose attached to the four-linked position of the threearm mannose of N-linked core pentasaccharide. These preliminary findings suggest that the specific glycoform of Hp may be useful as a marker to monitor lung cancer progression.
Hepatitis B virus (HBV) X protein (HBx) plays a key role in the development of hepatocellular car... more Hepatitis B virus (HBV) X protein (HBx) plays a key role in the development of hepatocellular carcinoma (HCC) in HBV carriers. A drug that can bind to the promoter region of HBV may shut down the expression of HBx and subsequently prevent the development of HCC in the HBV carrier. We have constructed a seven amino acid residue peptide library on a TentaGel resin using a combinatorial one-bead one-sequence peptide synthesis method. The fluorescently labeled eicosanucleotide (5¢-(6-FAM) CTTTTGGGCT TTGCTGCCCC-3¢) of the HBx promoter region was used as a monitor to screen for peptides that have high binding affinity to the HBx promoter. Two heptapeptides, KAPLFSI and SRVRMTW, were identified, and synthesized. The binding affinities of the peptides to the HBx promoter oligonucleotide were determined using Surface Plasmon Resonance (SPR). The peptide KAPLFSI had a greater binding affinity constant (k a ) and equilibrium constant (K D ) than SRVRMTW. The k a and K D values with the full X-promoter sequence were found to be 1.425 E+5 (1/Ms) and 1.186 E-8 (M), respectively. The peptide may open a new route for tumor suppression in HBV carriers. . Biacore Sensorgrams of the interactions between the peptide sequence KAPLFSI and the X-promoter oligonucleotide sequences at different concentrations.
Glycosylation is a common protein modification that is of interest in current cancer research bec... more Glycosylation is a common protein modification that is of interest in current cancer research because altered carbohydrate moieties are often found during cancer progress. A search for biomarkers in human lung cancer serum samples using glycoproteomic approaches identified fucosylated haptoglobin (Hp) significantly increased in serum of each subtype of lung cancer compared to normal donors. In addition, MS provided evidence of an increase of Hp fucosylation; the glycan structure was determined to be an a 2,6-linked tri-sialylated triantennary glycan containing a1,3-linked fucose attached to the four-linked position of the threearm mannose of N-linked core pentasaccharide. These preliminary findings suggest that the specific glycoform of Hp may be useful as a marker to monitor lung cancer progression.