Membrane destabilization by monomeric hIAPP observed by imaging fluorescence correlation spectroscopy

被引：35

作者：

Bag, Nirmalya ^{[1
,2
,3
]}

Ali, Ashraf ^{[4
]}

Chauhan, Virander Singh ^{[4
]}

Wohland, Thorsten ^{[1
,2
,3
]}

Mishra, Aseem ^{[4
]}

机构：

[1] Natl Univ Singapore, Dept Biol Sci, Singapore 117557, Singapore

[2] Natl Univ Singapore, Dept Chem, Singapore 117557, Singapore

[3] Natl Univ Singapore, NUS Ctr Bioimaging Sci CBIS, Singapore 117557, Singapore

[4] Int Ctr Genet Engn & Biotechnol, Malaria Res Grp, New Delhi 110067, India

来源：

CHEMICAL COMMUNICATIONS | 2013年 / 49卷 / 80期

关键词：

ISLET AMYLOID POLYPEPTIDE; DIFFUSION; ORGANIZATION;

D O I：

10.1039/c3cc44880k

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Monomeric hIAPP significantly destabilizes both model and live cell membranes by increasing membrane fluidity. This interaction with membranes happens via carpet formation followed by lipid extraction in a concentration dependent manner and thus we propose that hIAPP aggregation prior to membrane interaction may not be necessary for its cytotoxicity.

引用

页码：9155 / 9157

页数：3

共 16 条

[1] Calibration and Limits of Camera-Based Fluorescence Correlation Spectroscopy: A Supported Lipid Bilayer Study [J].

Bag, Nirmalya ;

Sankaran, Jagadish ;

Paul, Alexandra ;

Kraut, Rachel S. ;

Wohland, Thorsten .

CHEMPHYSCHEM, 2012, 13 (11) :2784-2794

[2] Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers [J].

Domanov, Yegor A. ;

Kinnunen, Paavo K. J. .

JOURNAL OF MOLECULAR BIOLOGY, 2008, 376 (01) :42-54

[3] Amphipathic helices and membrane curvature [J].

Drin, Guillaume ;

Antonny, Bruno .

FEBS LETTERS, 2010, 584 (09) :1840-1847

[4] Monte Carlo simulations of peptide-membrane interactions with the MCPep web server [J].

Gofman, Yana ;

Haliloglu, Turkan ;

Ben-Tal, Nir .

NUCLEIC ACIDS RESEARCH, 2012, 40 (W1) :W358-W363

[5] A Fluorescent Pentameric Thiophene Derivative Detects in Vitro-Formed Prefibrillar Protein Aggregates [J].

Hammarstrom, Per ;

Simon, Rozalyn ;

Nystrom, Sofie ;

Konradsson, Peter ;

Aslund, Andreas ;

Nilsson, K. Peter R. .

BIOCHEMISTRY, 2010, 49 (32) :6838-6845

[6] The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles [J].

Janson, J ;

Ashley, RH ;

Harrison, D ;

McIntyre, S ;

Butler, PC .

DIABETES, 1999, 48 (03) :491-498

[7] Islet amyloid polypeptide demonstrates a persistent capacity to disrupt membrane integrity [J].

Last, Nicholas B. ;

Rhoades, Elizabeth ;

Miranker, Andrew D. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (23) :9460-9465

[8] Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide [J].

Magzoub, Mazin ;

Miranker, Andrew D. .

FASEB JOURNAL, 2012, 26 (03) :1228-1238

[9] Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies [J].

Mao, Xiao-Bo ;

Wang, Chen-Xuan ;

Wu, Xing-Kui ;

Ma, Xiao-Jing ;

Liu, Lei ;

Zhang, Lan ;

Niu, Lin ;

Guo, Yuan-Yuan ;

Li, Deng-Hua ;

Yang, Yan-Lian ;

Wang, Chen .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2011, 108 (49) :19605-19610

[10] OPINION Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations [J].

Melo, Manuel N. ;

Ferre, Rafael ;

Castanho, Miguel A. R. B. .

NATURE REVIEWS MICROBIOLOGY, 2009, 7 (03) :245-250

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