Studying antibiotic-membrane interactions via X-ray diffraction and fluorescence microscopy

Please use this identifier to cite or link to this item: https://ir.lib.ncu.edu.tw/handle/987654321/108141

Title:	Studying antibiotic-membrane interactions via X-ray diffraction and fluorescence microscopy
Authors:	李明道;Sun, Yi-Ting;Huang, Ping-Yuan;Lin, Cheng-Hao;Lee, Kuan-Rong;Lee, Ming-Tao
Contributors:	理學院物理學系
Keywords:	ABC transporters;antibiotic resistance;Antibiotics;Aqueous solutions;Bacteria;Bacterial infections;Cholesterol;Diffraction;Drug resistance;fluorescence microscopy;GUV;Hazardous materials;Humidity;Hydrophobicity;LXD;Membranes;Nosocomial infections;Penicillin;Proteins;Research article;Sulbactam;X-ray diffraction
Date:	2015-01-01
Issue Date:	2026-04-23 14:37:08 (UTC+8)
Publisher:	Wiley-Blackwell;England: Elsevier B.V
Abstract:	摘要： •We present antibiotic-induced membrane thinning of a multi-lamellar thin film sample.•Both penicillin and sulbactam are found positioned outside the model membrane in an aqueous solution.•We demonstrate a hybrid method to study the antibiotic–membrane interaction. Antibiotic drug resistance is a serious issue for the treatment of bacterial infection. Understanding the resistance to antibiotics is a key issue for developing new drugs. We used penicillin and sulbactam as model antibiotics to study their interaction with model membranes. Cholesterol was used to target the membrane for comparison with the well-known insertion model. Lamellar X-ray diffraction (LXD) was used to determine membrane thickness using successive drug-to-lipid molar ratios. The aspiration method for a single giant unilamellar vesicle (GUV) was used to monitor the kinetic binding process of antibiotic–membrane interactions in an aqueous solution. Both penicillin and sulbactam are found positioned outside the model membrane, while cholesterol inserts perpendicularly into the hydrophobic region of the membrane in aqueous solution. This result provides structural insights for understanding the antibiotic–membrane interaction and the mechanism of antibiotics. 其他題名： FEBS Open Bio 出版者： England: Elsevier B.V 出版日期： 2015-01-01 出處： FEBS open bio, 2015-01, Vol.5 (1), p.515-521 資源來源： Publicly available content database 版權： 2015 The Authors 版權： FEBS Open Bio 5 (2015) 2211-5463 ©2015 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. 版權： 2015. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 版權： 2015 The Authors 2015 識別號： ISSN: 2211-5463 識別號： EISSN: 2211-5463 識別號： DOI: 10.1016/j.fob.2015.06.006 識別號： PMID: 26155459
Appears in Collections:	[Department of Physics] journal & Dissertation

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