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从苏云金芽孢杆菌中存在的Cry1Ab16毒素分离出的肽:通过原子力显微镜研究的逐层薄膜的合成与形态学数据。

Peptide isolated from Cry1Ab16 toxin present in Bacillus thuringiensis: Synthesis and morphology data for layer-by-layer films studied by atomic force microscopy.

作者信息

Plácido Alexandra, de Oliveira Farias Emanuel Airton, Marani Mariela M, Gomes Vasconcelos Andreanne, Leite José R S A, Delerue-Matos Cristina

机构信息

REQUIMTE/LAQV, Instituto Superior de Engenharia do Porto, ISEP, Instituto Politécnico do Porto, Porto, Portugal.

Núcleo de Pesquisa em Biodiversidade e Biotecnologia, BIOTEC, Campus Ministro Reis Velloso, CMRV, Universidade Federal do Piauí, UFPI, Parnaíba, PI, Brasil.

出版信息

Data Brief. 2016 May 21;8:114-9. doi: 10.1016/j.dib.2016.05.031. eCollection 2016 Sep.

DOI:10.1016/j.dib.2016.05.031
PMID:27294178
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4889891/
Abstract

The peptide PcL342-354C was obtained from the Cry1Ab16 toxin present in Bacillus thuringiensis ("Computational Modeling Deduced Three Dimensional Structure of Cry1Ab16 Toxin from B. thuringiensis AC11" (Kashyap, 2012) [1]). In this data article, we report the synthesis and characterization of the PcL342-354C peptide by MALDI-TOF/TOF mass spectrometry. In addition, the preparation of layer-by-layer films is shown based on interspersion of this peptide with both polyethylenimine (PEI) and poly(sodium 4-styrenesulfonate) (PSS), self-assembled on ITO (indium tin oxide) electrodes. The morphology of the ITO/PEI/PSS/PcL342-354C film was analyzed using atomic force microscopy (AFM). We also evaluated the effect of the number of bilayers in ITO/PEI/(PSS/PcL342-354C) n on the morphology of the film using AFM amplitude images. Further details about this study were published elsewhere, "Layer-by-layer films containing peptides of the Cry1Ab16 toxin from B. thuringiensis for potential biotechnological applications," (Plácido et al., 2016) [2].

摘要

肽段PcL342 - 354C是从苏云金芽孢杆菌中存在的Cry1Ab16毒素获得的(“Computational Modeling Deduced Three Dimensional Structure of Cry1Ab16 Toxin from B. thuringiensis AC11”(Kashyap,2012年)[1])。在本数据文章中,我们报告了通过基质辅助激光解吸电离飞行时间/串联飞行时间质谱对PcL342 - 354C肽段进行的合成与表征。此外,展示了基于该肽段与聚乙烯亚胺(PEI)和聚(4 - 苯乙烯磺酸钠)(PSS)的交替穿插,在氧化铟锡(ITO)电极上自组装制备逐层薄膜的过程。使用原子力显微镜(AFM)分析了ITO/PEI/PSS/PcL342 - 354C薄膜的形态。我们还使用AFM振幅图像评估了ITO/PEI/(PSS/PcL342 - 354C)n中双层数对薄膜形态的影响。关于这项研究的更多详细信息发表在其他地方,“Layer - by - layer films containing peptides of the Cry1Ab16 toxin from B. thuringiensis for potential biotechnological applications”(Plácido等人,2016年)[2]。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/2193f3295772/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/8488f72dd7a8/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/07b1f705d1fc/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/62ce0d801b96/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/2193f3295772/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/8488f72dd7a8/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/07b1f705d1fc/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/62ce0d801b96/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2cdd/4889891/2193f3295772/gr4.jpg

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本文引用的文献

1
Layer-by-layer films containing peptides of the Cry1Ab16 toxin from Bacillus thuringiensis for potential biotechnological applications.用于潜在生物技术应用的含有苏云金芽孢杆菌 Cry1Ab16 毒素肽的层层膜。
Mater Sci Eng C Mater Biol Appl. 2016 Apr 1;61:832-41. doi: 10.1016/j.msec.2016.01.011. Epub 2016 Jan 9.
2
Characterization and Biological Activities of Ocellatin Peptides from the Skin Secretion of the Frog Leptodactylus pustulatus.爪蟾皮肤分泌物中卵母细胞成熟因子肽的特性和生物学活性。
J Nat Prod. 2015 Jul 24;78(7):1495-504. doi: 10.1021/np500907t. Epub 2015 Jun 24.
3
Computational Modeling Deduced Three Dimensional Structure of Cry1Ab16 Toxin from Bacillus thuringiensis AC11.
计算建模推导出苏云金芽孢杆菌 AC11 中 Cry1Ab16 毒素的三维结构。
Indian J Microbiol. 2012 Jun;52(2):263-9. doi: 10.1007/s12088-011-0191-5. Epub 2011 Jun 26.
4
A critical reappraisal of Waddell's technique for ultraviolet spectrophotometric protein estimation.对瓦德尔紫外分光光度法蛋白质测定技术的批判性重新评估。
Anal Biochem. 1983 Feb 15;129(1):145-55. doi: 10.1016/0003-2697(83)90062-3.