Temperature Dependent AFM of Single Lipid and Mixed Lipid-Peptide Bilayers

F. Yarrow; J. P. J. M. van der Eerden; M. M. E. Snel

doi:10.1063/1.1639728

Temperature Dependent AFM of Single Lipid and Mixed Lipid-Peptide Bilayers

F. Yarrow
, J. P. J. M. van der Eerden
, M. M. E. Snel

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Regularly striped patterns are observed when imaging supported, mixed bilayers of the phospholipid DPPC and a synthetic α-helical transmembrane peptide (WALP) with contact mode AFM at ambient temperature. Temperature dependent AFM is used here as a tool to observe the temperature behavior of this system. Melting in a 2 mol% peptide/DPPC system starts at 36°C. The domains lie higher than the surrounding lipid bilayer at low temperatures (<36°C), but change to lower lying areas above that temperature. In contrast, pure lipid bilayers do not start melting until 40.5°C. Melting seems to start at defects present in the lipid bilayer.

Original language	English
Pages (from-to)	416-421
Journal	AIP Conference Proceedings
Volume	696
DOIs	https://doi.org/10.1063/1.1639728
Publication status	Published - 1 Dec 2003

Keywords

Lipids
Membranes bilayers and vesicles
Scanning tunneling and atomic force microscopy

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10.1063/1.1639728

http://adsabs.harvard.edu/abs/2003AIPC..696..416Y

Cite this

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title = "Temperature Dependent AFM of Single Lipid and Mixed Lipid-Peptide Bilayers",

abstract = "Regularly striped patterns are observed when imaging supported, mixed bilayers of the phospholipid DPPC and a synthetic α-helical transmembrane peptide (WALP) with contact mode AFM at ambient temperature. Temperature dependent AFM is used here as a tool to observe the temperature behavior of this system. Melting in a 2 mol\% peptide/DPPC system starts at 36°C. The domains lie higher than the surrounding lipid bilayer at low temperatures (<36°C), but change to lower lying areas above that temperature. In contrast, pure lipid bilayers do not start melting until 40.5°C. Melting seems to start at defects present in the lipid bilayer.",

keywords = "Lipids, Membranes bilayers and vesicles, Scanning tunneling and atomic force microscopy",

author = "F. Yarrow and \{van der Eerden\}, \{J. P. J. M.\} and Snel, \{M. M. E.\}",

year = "2003",

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doi = "10.1063/1.1639728",

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journal = "AIP Conference Proceedings",

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AU - Yarrow, F.

AU - van der Eerden, J. P. J. M.

AU - Snel, M. M. E.

PY - 2003/12/1

Y1 - 2003/12/1

N2 - Regularly striped patterns are observed when imaging supported, mixed bilayers of the phospholipid DPPC and a synthetic α-helical transmembrane peptide (WALP) with contact mode AFM at ambient temperature. Temperature dependent AFM is used here as a tool to observe the temperature behavior of this system. Melting in a 2 mol% peptide/DPPC system starts at 36°C. The domains lie higher than the surrounding lipid bilayer at low temperatures (<36°C), but change to lower lying areas above that temperature. In contrast, pure lipid bilayers do not start melting until 40.5°C. Melting seems to start at defects present in the lipid bilayer.

AB - Regularly striped patterns are observed when imaging supported, mixed bilayers of the phospholipid DPPC and a synthetic α-helical transmembrane peptide (WALP) with contact mode AFM at ambient temperature. Temperature dependent AFM is used here as a tool to observe the temperature behavior of this system. Melting in a 2 mol% peptide/DPPC system starts at 36°C. The domains lie higher than the surrounding lipid bilayer at low temperatures (<36°C), but change to lower lying areas above that temperature. In contrast, pure lipid bilayers do not start melting until 40.5°C. Melting seems to start at defects present in the lipid bilayer.

KW - Lipids

KW - Membranes bilayers and vesicles

KW - Scanning tunneling and atomic force microscopy

U2 - 10.1063/1.1639728

DO - 10.1063/1.1639728

M3 - Article

SN - 0094-243X

VL - 696

SP - 416

EP - 421

JO - AIP Conference Proceedings

JF - AIP Conference Proceedings

ER -

Temperature Dependent AFM of Single Lipid and Mixed Lipid-Peptide Bilayers

Abstract

Keywords

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