Publications (5)33 Total impact
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Article: Self-Adjuvanting Synthetic Antitumor Vaccines from MUC1 Glycopeptides Conjugated to T-Cell Epitopes from Tetanus Toxoid.
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ABSTRACT: The T-helper epitope peptide P30 (green in the scheme) from tetanus toxoid was used as the immunostimulant in MUC1 glycopeptide antitumor vaccines and apparently also acts as a built-in adjuvant. P30-conjugated glycopeptide vaccines containing three glycans in the immunodominant motifs PDTRP and GSTAP induced much stronger immune responses and complement dependent cytotoxicity mediated killing of tumor cells when applied in plain PBS solution without complete Freund's adjuvant.Angewandte Chemie International Edition 04/2013; · 13.45 Impact Factor -
Article: Characterizing the assembly behaviors of human amylin: a perspective derived from C-terminal variants.
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ABSTRACT: The differences in the C-terminal domains of human amylin peptide variants initiate different aggregation processes and differences in the composition of the aggregates by affecting the hydrophobic cores, conformations, and intra-sheet interactions of the peptides, which have distinct effects on the cytotoxicity of the peptides.Chemical Communications 11/2012; · 6.17 Impact Factor -
Article: Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin.
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ABSTRACT: The pathogenesis of type II diabetes can be linked to cosecreted hIAPP/insulin interacting with cell membranes. Here we investigate the nanostructures by co-assembling hIAPP and insulin on surfaces. By tuning the hIAPP/insulin ratio, atomic force microscopy reveals the resulting nanostructure morphology changes from fibrils to oligomers, to annular. Implications for in vivo studies are discussed.Chemical Communications 01/2012; 48(2):191-3. · 6.17 Impact Factor -
Article: Hybrid peptides attenuate cytotoxicity of beta-amyloid by inhibiting its oligomerization: implication from solvent effects.
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ABSTRACT: Abnormal assembly of monomeric beta-amyloid (Abeta) in Alzheimer's disease leads to the formation of most neurotoxic oligomers in vivo. In this study, we explored a linking strategy to design hybrid peptides, by combining the Abeta recognition motif and the solvent disruptive sequences. We found that in vitro all synthetic peptides with the recognition motif can affect Abeta fibrillization and alter the morphology of Abeta aggregates variously, different from those without the recognition motif. The effects of peptides containing recognition motif on Abeta aggregation correlate with their abilities to change the surface tension of solutions. In addition, compounds with the recognition motif, not those without such motif, can inhibit cytotoxicity of Abeta in cell culture probably by decreasing the amount of toxic Abeta oligomers. These results indicate that recognition domain and solvent effect should be considered as important factors when designing molecules to target Abeta aggregation.Peptides 05/2009; 30(7):1282-7. · 2.43 Impact Factor -
Article: Sequestration of copper from beta-amyloid promotes selective lysis by cyclen-hybrid cleavage agents.
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ABSTRACT: Decelerated degradation of beta-amyloid (Abeta) and its interaction with synaptic copper may be pathogenic in Alzheimer disease. Recently, Co(III)-cyclen tagged to an aromatic recognition motif was shown to degrade Abeta in vitro. Here, we report that apocyclen attached to selective Abeta recognition motifs (KLVFF or curcumin) can capture copper bound to Abeta and use the Cu(II) in place of Co(III) to become proteolytically active. The resultant complexes interfere with Abeta aggregation, degrade Abeta into fragments, preventing H2O2 formation and toxicity in neuronal cell culture. Because Abeta binds Cu in amyloid plaques, apocyclen-tagged targeting molecules may be a promising approach to the selective degradation of Abeta in Alzheimer disease. The principle of copper capture could generalize to other amyloidoses where copper is implicated.Journal of Biological Chemistry 09/2008; 283(46):31657-64. · 4.77 Impact Factor
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Institutions
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2008–2009
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Tsinghua University
- Department of Chemistry
Beijing, Beijing Shi, China
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