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Carbon Nanotubes Induce Secondary Structure Changes of Bovine Albumin in Aqueous Phase
Yang, M; Meng, J; Mao, XB; Yang, Y; Cheng, XL; Yuan, H; Wang, C; Xu, HY; Yuan H(袁慧)
2010
Source PublicationJOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY
Volume10Issue:11Pages:7550-7553
Corresponding Author[Mao, Xiaobo ; Yang, Yang ; Wang, Chen] Nat Ctr Nanosci & Technol, Beijing 100080, Peoples R China ; [Yang, Man ; Meng, Jie ; Cheng, Xuelian ; Xu, Haiyan] Chinese Acad Med Sci, Inst Basic Med Sci, Beijing 100005, Peoples R China ; [Yang, Man ; Meng, Jie ; Cheng, Xuelian ; Xu, Haiyan] Peking Union Med Coll, Beijing 100005, Peoples R China ; [Yuan, Hui] Chinese Acad Sci, Inst High Energy Phys, Beijing 100049, Peoples R China
SubtypeArticle; Proceedings Paper
AbstractInteraction of nanomaterials to protein molecules is one of the most important issues to deeply understand the influences of the nanomaterials upon physiological processes and protein functions. So far most of investigations focused on the protein molecules adsorbed on the nanomaterials surface, less is known about those in the aqueous phase (not absorbed). In this work, luminescent spectroscopy analysis, circular dichroism measurement, atomic force microscopy, matrix-assisted laser desorption/ionization time of flight mass spectrometry, isoelectric focusing and sulfate polyacrylamide gel electrophoresis were used to investigate the influence of oxidized water-soluble multiwalled carbon nanotubes (CNT) dispersing in aqueous solution upon the structures of bovine serum albumin (BSA) through co-incubation. We focused on BSA molecules that stayed in the aqueous phase instead of those adsorbed by CNT. Experimental results show that the fractions of beta-sheet decreased from 33.3% to 29.8% and beta-turn increased from 2% to 5% in reference with native BSA. There was a slight increase of alpha-helix and a slight reduction of random coil. BSA molecules that had been encountered with CNT and were left in the solution formed a loose and flatten morphology on graphite substrates instead of their native tight and round morphology observed by AFM. The value of isoelectric point for BSA after exposed to CNT moved towards to a higher pH position compared with native BSA. All together, it was concluded that the oxidized water-soluble multiwalled carbon nanotubes not only adsorb bovine serum albumin molecules to their surface, but also induces albumin molecules in the aqueous solution undergo secondary structure changes, which lead to a conformation change.
KeywordCarbon Nanotubes Protein Interaction Secondary Structure Aqueous Phase
Subject AreaChemistry; Science & Technology - Other Topics; Materials Science; Physics
DOI10.1166/jnn.2010.2825
URL查看原文
Indexed BySCI
Language英语
WOS Research AreaChemistry ; Science & Technology - Other Topics ; Materials Science ; Physics
WOS SubjectChemistry, Multidisciplinary ; Nanoscience & Nanotechnology ; Materials Science, Multidisciplinary ; Physics, Applied ; Physics, Condensed Matter
WOS IDWOS:000283621300129
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Document Type期刊论文
Identifierhttp://ir.ihep.ac.cn/handle/311005/240123
Collection多学科研究中心
Affiliation中国科学院高能物理研究所
First Author AffilicationInstitute of High Energy
Recommended Citation
GB/T 7714
Yang, M,Meng, J,Mao, XB,et al. Carbon Nanotubes Induce Secondary Structure Changes of Bovine Albumin in Aqueous Phase[J]. JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY,2010,10(11):7550-7553.
APA Yang, M.,Meng, J.,Mao, XB.,Yang, Y.,Cheng, XL.,...&袁慧.(2010).Carbon Nanotubes Induce Secondary Structure Changes of Bovine Albumin in Aqueous Phase.JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY,10(11),7550-7553.
MLA Yang, M,et al."Carbon Nanotubes Induce Secondary Structure Changes of Bovine Albumin in Aqueous Phase".JOURNAL OF NANOSCIENCE AND NANOTECHNOLOGY 10.11(2010):7550-7553.
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