硫硒化镉纳米颗粒对胰高血糖素聚集的影响
PDF下载 (383)李春草1,徐 鹏1,王兰杰1,魏余辉1,孔丽霞1,李 宾2,周星飞1*.硫硒化镉纳米颗粒对胰高血糖素聚集的影响[J].宁波大学学报(理工版),2016,29(1):69-72.DOI:
LI Chun-cao1,XU Peng1,WANG Lan-jie1,WEI Yu-hui1,KONG Li-xia1,LI Bin2,ZHOU Xing-fei1*.Effect of Cadmium Selenide Sulfide Nanoparticles on Glucagon Aggregation[J].Journal of Ningbo University(Natural Science & Engineering Edition),2016,29(1):69-72.DOI:
| Title: | Effect of Cadmium Selenide Sulfide Nanoparticles on Glucagon Aggregation |
| 作者: | 李春草1, 徐 鹏1, 王兰杰1, 魏余辉1, 孔丽霞1, 李 宾2, 周星飞1* |
| Author(s): | LI Chun-cao1, XU Peng1, WANG Lan-jie1, WEI Yu-hui1, KONG Li-xia1, LI Bin2, ZHOU Xing-fei1* |
| 关键词: | 硫硒化镉纳米颗; 胰高血糖素; 原子力显微镜; 纤维化 |
| Keywords: | CdSeS NPs; Glucagon; AFM; Fibrillation |
| 分类号: | O629.8 |
| 文献标识码: | A |
| 摘要: | 利用原子力显微镜、傅里叶变换红外光谱仪和荧光光度计等研究了硫硒化镉纳米颗粒对胰高血糖素聚集的影响, 包括聚集形成纤维数量的多少、纤维的生长速度等. 结果表明: 硫硒化镉纳米颗粒能够抑制胰高血糖素多肽的聚集, 并且随着颗粒浓度的增加, 其抑制胰高血糖素维化的程度也明显加剧. 另外, 还对纳米颗粒抑制胰高血糖素聚集的机理进行了初步讨论. |
| Abstract: | In this paper, we have investigated the effect of Cadmium Selenide Sulfide nanoparticles (CdSeS NPs) on the fibrillation of glucagon peptides using AFM, FTIR and Fluorophotometer. We have found that CdSeS NPs can inhibit glucagon peptide aggregation progress which is strongly dependent on the concentration of CdSeS NPs. In addition, the mechanism of interaction between glucagon and NPs is also discussed. |
| 参考文献 /References: | [1].KUMAR S, UDGAONKAR J B. Mechanisms of amyloid fibril formation proteins[J]. Curr Sci, 2010, 98(5):639-656. [2].CHITI F, DOBSON C M. Protein misfolding, functional amyloid, and human disease[J]. Annu Rev Biochem, 2006, 75:333-366. [3].DETOMA A S, SALAMEKH S, RAMAMOORTHY A, et al. Misfolded proteins in alzheimer’s disease and type II diabetes[J]. Chem Soc Rev, 2012, 41(5):608-621. [4].翟彩宁, 贺静, 毛新焕, 等. 金属离子对牛胰岛素淀粉样纤维形成的作用[J]. 四川大学学报, 2008, 45(6):1499- 1503. [5].王志刚, 万立俊, 周纯青, 等. β-淀粉样蛋白在石墨表面吸附及凝聚结构的STM和AFM研究[J]. 科学通报, 2002, 47(12):908-911. [6].SAHIN E, GRILLO A O, PERKINS M D, et al. Comparative effects of pH and ionic strength on protein- protein interactions, unfolding, and aggregation for IgG1 antibodies[J]. J Pharm Sci, 2010, 99(12):4830-4848. [7].GORBENKO G P, KINNUNEN P K J. The role of lipid-protein interactions in amyloid-type protein fibril formation[J]. Chem Phys Lipids, 2006, 141(1/2):72-82. [8].ZHANG L, ZHONG J, HUANG L X, et al. Parallel-oriented fibrogenesis of a β-sheet forming peptide on supported lipid bilayers[J]. J Phys Chem B, 2008, 112(30):8950- 8954. [9].MORRISS A A, BROWN F L H, SHEA J E. A coarse- grained model for peptide aggregation on a membrane surface[J]. J Phys Chem B, 2014, 118(28):8420-8432. [10].ZHOU X F, TAN J H, ZHENG L F, et al. The opposite effects of Cu(II) and Fe(III) on the assembly of glucagon amyloid fibrils[J]. RSC Adv, 2012, 2(12):5418-5423. [11].ALVAREZ Y D, FAUERBACH J A, PELLEGROTTI J V, et al. Influence of gold nanoparticles on the kinetics of α-synuclein[J]. Nano Lett, 2013, 13(12):6156-6163. [12].WU W H, SUN X, YU Y P, et al. TiO2 nanoparticles promote β-amyloid fibrillation in vitro[J]. Biochem Biophys Res Commun, 2008, 373:315-318. [13].CABALEIRO L C, QUINLAN P F, LYNCH I, et al. Inhi- bition of amyloid β protein fibrillation by polymeric nano- particles[J]. J Am Chem Soc, 2008, 130(46):15437-15443. [14].HIRAMATSU H, KITAGAWA T. FT-IR approaches on amyloid fibril structure[J]. Biochimica et Biophysica Acta, 2005, 1753(1):100-107. [15].LINSE S, CABALEIRO L C, XUE W F, et al. Nucleation of protein fibrillation by nanoparticles[J]. Proc Natl Acad Sci USA, 2007, 104(21):8691-8696. [16].BRAMBILLA D, VERPILLOT R, LEDROUMAGUET B, et al. PEGylated nanoparticles bind to and alter amyloid-beta peptide conformation: Toward engineering of functional nanomedicines for alzheimer’s disease[J]. ACS Nano, 2012, 6(7):5897-5908. [17].COLVIN V L, KULINOWSKI K M. Nanoparticles as catalysts for protein fibrillation[J]. Proc Natl Acad Sci USA, 2007, 104(21):8679-8680. [18].BELLOVA A, BYSTRENOVA E, KONERACKA M, et al. Effect of Fe3O4 magnetic nanoparticles on lysozyme amyloid aggregation[J]. Nanotechnology, 2010, 21(6): 65103-65109. [19].SKAAT H, CHEN R, GRINBERG I, et al. Engineered polymer nanoparticles containing hydrophobic dipeptide for inhibition of amyloid-β fibrillation[J]. Biomacromole- cules, 2012, 13(9):2662-2670. |
| 备注/Memo: | 收稿日期: 2014?12?17. 宁波大学学报(理工版)网址: http://journallg.nbu.edu.cn/ 基金项目: 国家自然科学基金( 11474173 ) ; 浙江省自然科学基金( Y14A040006 ) ; 宁波大学王宽诚教育基金 . 第一作者: 李春草(1987-), 女, 安徽亳州人, 在读硕士研究生, 主要研究方向: 颗粒对多肽聚集的影响. E-mail: m15257495315@163.com * 通信作者: 周星飞( 1963 -) , 男 , 浙江余姚人 , 副研究员 , 主要研究方向 : 蛋白分子的自组装 . E-mail: zhouxingfei@nbu.edu.cn 宁波大学学报(理工版)网址:http://journallg.nbu.edu.cn/ |