The solution structure of the active domain of CAP18 - a lipopolysaccharide binding protein from rabbit leukocytes

Chinpan Chen; Roland Brock; Frederick Luh; Ping Jung Chou; James W. Larrick; Rong Fong Huang; Tai huang Huang

doi:10.1016/0014-5793(95)00792-8

The solution structure of the active domain of CAP18 - a lipopolysaccharide binding protein from rabbit leukocytes

Chinpan Chen, Roland Brock, Frederick Luh, Ping Jung Chou, James W. Larrick, Rong Fong Huang, Tai huang Huang^*

^*Corresponding author for this work

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

66 Citations (Scopus)

Abstract

We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18_106-137, a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18_106-137 may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18_106-137 in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18_106-137 are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains.

Original language	English
Pages (from-to)	46-52
Number of pages	7
Journal	FEBS Letters
Volume	370
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(95)00792-8
Publication status	Published - 1995 Aug 14
Externally published	Yes

Keywords

Antibacterial peptide
Endotoxin
Lipid A
NMR

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(95)00792-8

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title = "The solution structure of the active domain of CAP18 - a lipopolysaccharide binding protein from rabbit leukocytes",

abstract = "We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18106-137, a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18106-137 may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18106-137 in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18106-137 are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains.",

keywords = "Antibacterial peptide, Endotoxin, Lipid A, NMR",

author = "Chinpan Chen and Roland Brock and Frederick Luh and Chou, {Ping Jung} and Larrick, {James W.} and Huang, {Rong Fong} and Huang, {Tai huang}",

note = "Funding Information: Acknowledgments. This work is supported by a grant from the National Science Council of the Republic of China (N SC83-0203-B001-102). We thank Mr. Jen-Ning Yang for performing CD spectral calibration.",

year = "1995",

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doi = "10.1016/0014-5793(95)00792-8",

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volume = "370",

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journal = "FEBS Letters",

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T1 - The solution structure of the active domain of CAP18 - a lipopolysaccharide binding protein from rabbit leukocytes

AU - Chen, Chinpan

AU - Brock, Roland

AU - Luh, Frederick

AU - Chou, Ping Jung

AU - Larrick, James W.

AU - Huang, Rong Fong

AU - Huang, Tai huang

N1 - Funding Information: Acknowledgments. This work is supported by a grant from the National Science Council of the Republic of China (N SC83-0203-B001-102). We thank Mr. Jen-Ning Yang for performing CD spectral calibration.

PY - 1995/8/14

Y1 - 1995/8/14

N2 - We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18106-137, a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18106-137 may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18106-137 in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18106-137 are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains.

AB - We have employed the circular dichroism (CD) technique to characterize the solution structure of CAP18106-137, a lipopolysaccharide (LPS) binding, antimicrobial protein, and its interaction with lipid A. Our results revealed that CAP18106-137 may exist in at least three lipid A concentration-dependent, primarily helix conformations. The 'model' structure of CAP18106-137 in 30% (v/v) TFE, determined by nuclear magnetic resonance (NMR) technique, was found to be a complete and very rigid helix. In this conformation, the cationic and hydrophobic groups of CAP18106-137 are separated into patches and stripes in such a way that it can favorably interact with lipid A through either coulombic interaction with the diphosphoryl groups or hydrophobic interaction with the fatty acyl chains.

KW - Antibacterial peptide

KW - Endotoxin

KW - Lipid A

KW - NMR

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SN - 0014-5793

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JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

The solution structure of the active domain of CAP18 - a lipopolysaccharide binding protein from rabbit leukocytes

Abstract

Keywords

ASJC Scopus subject areas

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