【摘 要】
：
Epithelial cancer-associated MUC1 glycoprotein serves as an attractive and broadly applicable target for cancer immunotherapy, which contains a variable number of tandem repeats (VNTR).The VNTR compri
【机 构】
：
CAS Key Laboratory for Biological Effects of Nanomaterials and Nanosafety, National Center for Nanos
【出 处】
：
The 9th Asian Biophysics Association Symposium (ABA2015)(第九届
论文部分内容阅读
Epithelial cancer-associated MUC1 glycoprotein serves as an attractive and broadly applicable target for cancer immunotherapy, which contains a variable number of tandem repeats (VNTR).The VNTR comprises a 20-amino acid extracellular domain with the sequence HGVTS APDTR PAPGS TAPPA bearing tumor-associated carbohydrate antigens, such as Tn and STn.We investigated the coassembling characteristics of the naked VNTR (n-VNTR)/4, 4-bipyridyl (4Bpy) and the glycosylated VNTR (g-VNTR)/4Bpy on the highly oriented pyrolytic graphite (HOPG) surface with scanning tunneling microscopy.It demonstrates that both interact with each other to form the beta-sheet structures.However, n-VNTR peptides co-assembly with 4Bpy molecules in good order and the distribution of the stable lengths of n-VNTR peptides have a single peak at 4.55 nanometers, which means n-VNTR fold at the seventh site.While the g-VNTR peptides do not coassembly orderly in a large scale and have a wider length distribution than n-VNTR peptides.It reveals that the glycosylation gives rise to the instability for peptide assembly, which leads to the oligosaccharyl moieties exposing to benefit the signal transduction.It would deepen the understanding of the relationship between the sequence and the folding structure/biological function and give inspirations to the peptide/ protein vaccine design.
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