Lipid membrane binding of NK-lysin

Jean Marie Ruysschaert; Erik Goormaghtigh; F. Homblé; Mats Andersson; Edvards Liepinsh; Gottfried Otting

doi:10.1016/S0014-5793(98)00261-0

Lipid membrane binding of NK-lysin

Jean Marie Ruysschaert^*, Erik Goormaghtigh, F. Homblé, Mats Andersson, Edvards Liepinsh, Gottfried Otting

^*Corresponding author for this work

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

60 Citations (Scopus)

Abstract

The membrane-binding properties and pore-forming potential of the tumor-lysing and antibacterial polypeptide NK-lysin were investigated. Fluorescence quenching experiments show a drastic change of accessibility to Trp⁵⁸ in solution and in association with a lipid membrane. Calcein release from large unilamellar vesicles and fluctuating conductivity observed across a planar lipid bilayer of asolectin show that NK-lysin renders lipid bilayers permeable in a transient fashion, indicating a nonspecific lipid interaction as the mechanism underlying the biological activity. FTIR experiments show the same amount and type of regular secondary structure of NK-lysin in the membrane as in aqueous solution and exclude a structural rearrangement into a set of parallel or antiparallel α-helices as the predominant conformation. The molecular mechanism of the membrane-destabilizing effect of NK-lysin is discussed.

Original language	English
Pages (from-to)	341-344
Number of pages	4
Journal	FEBS Letters
Volume	425
Issue number	2
DOIs	https://doi.org/10.1016/S0014-5793(98)00261-0
Publication status	Published - 27 Mar 1998
Externally published	Yes

Access to Document

10.1016/S0014-5793(98)00261-0

Cite this

@article{002c59647cf048caae935dc1e9e17865,

title = "Lipid membrane binding of NK-lysin",

abstract = "The membrane-binding properties and pore-forming potential of the tumor-lysing and antibacterial polypeptide NK-lysin were investigated. Fluorescence quenching experiments show a drastic change of accessibility to Trp58 in solution and in association with a lipid membrane. Calcein release from large unilamellar vesicles and fluctuating conductivity observed across a planar lipid bilayer of asolectin show that NK-lysin renders lipid bilayers permeable in a transient fashion, indicating a nonspecific lipid interaction as the mechanism underlying the biological activity. FTIR experiments show the same amount and type of regular secondary structure of NK-lysin in the membrane as in aqueous solution and exclude a structural rearrangement into a set of parallel or antiparallel α-helices as the predominant conformation. The molecular mechanism of the membrane-destabilizing effect of NK-lysin is discussed.",

keywords = "Fourier transform infrared spectroscopy, Membrane binding, NK-lysin, Pore formation",

author = "Ruysschaert, \{Jean Marie\} and Erik Goormaghtigh and F. Hombl{\'e} and Mats Andersson and Edvards Liepinsh and Gottfried Otting",

year = "1998",

month = mar,

day = "27",

doi = "10.1016/S0014-5793(98)00261-0",

language = "English",

volume = "425",

pages = "341--344",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley \& Sons Inc.",

number = "2",

}

TY - JOUR

T1 - Lipid membrane binding of NK-lysin

AU - Ruysschaert, Jean Marie

AU - Goormaghtigh, Erik

AU - Homblé, F.

AU - Andersson, Mats

AU - Liepinsh, Edvards

AU - Otting, Gottfried

PY - 1998/3/27

Y1 - 1998/3/27

N2 - The membrane-binding properties and pore-forming potential of the tumor-lysing and antibacterial polypeptide NK-lysin were investigated. Fluorescence quenching experiments show a drastic change of accessibility to Trp58 in solution and in association with a lipid membrane. Calcein release from large unilamellar vesicles and fluctuating conductivity observed across a planar lipid bilayer of asolectin show that NK-lysin renders lipid bilayers permeable in a transient fashion, indicating a nonspecific lipid interaction as the mechanism underlying the biological activity. FTIR experiments show the same amount and type of regular secondary structure of NK-lysin in the membrane as in aqueous solution and exclude a structural rearrangement into a set of parallel or antiparallel α-helices as the predominant conformation. The molecular mechanism of the membrane-destabilizing effect of NK-lysin is discussed.

AB - The membrane-binding properties and pore-forming potential of the tumor-lysing and antibacterial polypeptide NK-lysin were investigated. Fluorescence quenching experiments show a drastic change of accessibility to Trp58 in solution and in association with a lipid membrane. Calcein release from large unilamellar vesicles and fluctuating conductivity observed across a planar lipid bilayer of asolectin show that NK-lysin renders lipid bilayers permeable in a transient fashion, indicating a nonspecific lipid interaction as the mechanism underlying the biological activity. FTIR experiments show the same amount and type of regular secondary structure of NK-lysin in the membrane as in aqueous solution and exclude a structural rearrangement into a set of parallel or antiparallel α-helices as the predominant conformation. The molecular mechanism of the membrane-destabilizing effect of NK-lysin is discussed.

KW - Fourier transform infrared spectroscopy

KW - Membrane binding

KW - NK-lysin

KW - Pore formation

UR - https://www.scopus.com/pages/publications/0032571477

U2 - 10.1016/S0014-5793(98)00261-0

DO - 10.1016/S0014-5793(98)00261-0

M3 - Article

SN - 0014-5793

VL - 425

SP - 341

EP - 344

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

Lipid membrane binding of NK-lysin

Abstract

Access to Document

Other files and links

Fingerprint

Cite this