机构:[1]State Key Laboratory for Supramolecular Structure and Materials, Jilin UniVersity, No. 2699, Qianjin Street, Changchun 130012, China[2]Key Laboratory of Bioorganic Phosphorous Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua UniVersity, Beijing 100084, China[3]Sichuan Tumor Hospital and Institute, Chengdu 610041, China四川省肿瘤医院
Capsid proteins binding cell surface proteoglycans is a key early event in human papillomavirus (HPV) infection. The positively charged sequences at the C-terminus of the L1 protein and the N- and C-termini of the L2 protein of HPV-16 can efficiently bind to heparin receptors, which were characterized in the present study by quantitative isothermal titration calorimetry experiments primarily, fluorescence spectroscopy, and static right-angle light scattering. The binding constant, K, was at an order of magnitude of 10(7) M-1 for the two peptides at the N- and C-termini of HPV-16 L2 and segment b at the C-terminus of HPV-16 L1, while that for other L1 analogues were of a smaller order, illustrating that the heparin binding is a typical sequence-specific and -dependent phenomenon. These results suggest that, in addition to L1, the L2 protein may participate in cell surface attachment during HPV infection. Furthermore, the calorimetry results demonstrated that hydrophobic interactions and hydrogen bonding are involved in peptide binding to heparin in addition to the essential electrostatic interactions. Meanwhile, circular dichroism spectroscopy revealed that binding to heparin does not induce obvious secondary structural changes in the peptides.
基金:
Natural
Science Foundation of China (No. 20934002 and 20973073),
the National Basic Research Program (2007CB808006), Natural
Science Foundation of Jilin Province (No. 20070926-01), the
Programs for New Century Excellent Talents in University
(NCET) and the 111 Project (B06009) (to J.S., S.J., and Y.W.),
and the State Key Laboratory for Supramolecular Structure and
Materials, Jilin University (to X.Z.).
第一作者机构:[1]State Key Laboratory for Supramolecular Structure and Materials, Jilin UniVersity, No. 2699, Qianjin Street, Changchun 130012, China
通讯作者:
推荐引用方式(GB/T 7714):
Sun Jian,Yu Ji-Sheng,Jin Shi,et al.Interaction of Synthetic HPV-16 Capsid Peptides with Heparin: Thermodynamic Parameters and Binding Mechanism[J].JOURNAL OF PHYSICAL CHEMISTRY B.2010,114(30):9854-9861.doi:10.1021/jp1009719.
APA:
Sun, Jian,Yu, Ji-Sheng,Jin, Shi,Zha, Xiao,Wu, Yuqing&Yu, Zhiwu.(2010).Interaction of Synthetic HPV-16 Capsid Peptides with Heparin: Thermodynamic Parameters and Binding Mechanism.JOURNAL OF PHYSICAL CHEMISTRY B,114,(30)
MLA:
Sun, Jian,et al."Interaction of Synthetic HPV-16 Capsid Peptides with Heparin: Thermodynamic Parameters and Binding Mechanism".JOURNAL OF PHYSICAL CHEMISTRY B 114..30(2010):9854-9861