【摘 要】
：
Epithelial cancer-associated glycoprotein MUC1 serves as a promising and broadly applicable target for cancer immunotherapy, which contains a variable number of tandem repeats (VNTRs).The VNTR compris
【机 构】
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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 glycoprotein MUC1 serves as a promising and broadly applicable target for cancer immunotherapy, which contains a variable number of tandem repeats (VNTRs).The VNTR comprises a 20-amino acid extracellular domain with the sequence HGVTSAPDTRPAPGSTAPPA bearing tumor-associated carbohydrate antigens, such as Tn, T and STn.We investigated the assembling characteristics of the naked VNTR (n-VNTR) and the glycosylated VNTR with glycosylated residue Thr9 and Ser15 (g-VNTR) on the highly oriented pyrolytic graphite (HOPG) surface with scanning tunneling microscopy.In order to identify the C-terminal of the peptides, 4, 4-bipyridyl (4Bpy) was introduced as a co-assembling species because of the strong hydrogen bond between 4Bpy and carboxyl groups.The n-VNTR peptides co-assemble with 4Bpy molecules in highly ordered manner and the distribution of the stable lengths of n-VNTR peptides shows a sharp peak at 4.55 nm, which suggests that n-VNTR peptides fold at the residue Pro7.While the g-VNTR peptides do not co-assemble orderly in a large scale and present a wider length distribution than n-VNTR peptides.Two most probable lengths are around 1.62 and 3.57 nm respectively corresponding to 5 and 11 residues (Thr16 and Arg10).Folding around the glycosylated residue Ser1 5 reveals that glycosylation gives rise to instability for peptide assembly, which leads to the oligosaccharyl exposure favorable to the signal transduction.It deepens our insight of the relationship between the sequence and the folding structure/biological function and would give inspirations to the peptide/protein vaccine design.
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