Electrochemistry and spectroscopy study on the interaction of microperoxidase-11 with lipid membrane

Weimin Huang; Zheling Zhang; Xiaojun Han; Jilin Tang; Zhangquan Peng; Shaojun Dong; Erkang Wang

doi:10.1016/S0301-4622(01)00230-7

Electrochemistry and spectroscopy study on the interaction of microperoxidase-11 with lipid membrane

Weimin Huang
, Zheling Zhang
, Xiaojun Han
, Jilin Tang
, Zhangquan Peng
, Shaojun Dong
, Erkang Wang^*

^*Corresponding author for this work

CAS - Changchun Institute of Applied Chemistry

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

23 Scopus citations

Abstract

The interaction of microperoxidase-11 (MP11) with cationic lipid vesicles of didodecyldimethylammonium bromide (DDAB) induces an α-helical conformation from random coil conformations in solution and this change then makes heme macrocycle more distorted. DDAB-induced MP11 conformations were investigated by cyclic votammetry (CV), circular dichroism (CD) and UV-vis spectrometry. All results indicate that the binding of MP11 in solution to DDAB vesicles and the ordered structure formation are driven by mostly electrostatic interaction between negatively charged residues in the undecapeptide and positively charged lipid headgroups on the membrane surface. Upon binding to DDAB, its half-peak potential was also changed. The mechanism of the interaction between MP11 and DDAB was also discussed.

Original language	English
Pages (from-to)	165-173
Number of pages	9
Journal	Biophysical Chemistry
Volume	94
Issue number	1-2
DOIs	https://doi.org/10.1016/S0301-4622(01)00230-7
State	Published - 11 Dec 2001
Externally published	Yes

Keywords

Didodecyldimethylammonium bromide
Electrochemistry
Microperoxidase-11
Spectroscopy

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10.1016/S0301-4622(01)00230-7

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title = "Electrochemistry and spectroscopy study on the interaction of microperoxidase-11 with lipid membrane",

abstract = "The interaction of microperoxidase-11 (MP11) with cationic lipid vesicles of didodecyldimethylammonium bromide (DDAB) induces an α-helical conformation from random coil conformations in solution and this change then makes heme macrocycle more distorted. DDAB-induced MP11 conformations were investigated by cyclic votammetry (CV), circular dichroism (CD) and UV-vis spectrometry. All results indicate that the binding of MP11 in solution to DDAB vesicles and the ordered structure formation are driven by mostly electrostatic interaction between negatively charged residues in the undecapeptide and positively charged lipid headgroups on the membrane surface. Upon binding to DDAB, its half-peak potential was also changed. The mechanism of the interaction between MP11 and DDAB was also discussed.",

keywords = "Didodecyldimethylammonium bromide, Electrochemistry, Microperoxidase-11, Spectroscopy",

author = "Weimin Huang and Zheling Zhang and Xiaojun Han and Jilin Tang and Zhangquan Peng and Shaojun Dong and Erkang Wang",

year = "2001",

month = dec,

day = "11",

doi = "10.1016/S0301-4622(01)00230-7",

language = "英语",

volume = "94",

pages = "165--173",

journal = "Biophysical Chemistry",

issn = "0301-4622",

publisher = "Elsevier B.V.",

number = "1-2",

}

TY - JOUR

T1 - Electrochemistry and spectroscopy study on the interaction of microperoxidase-11 with lipid membrane

AU - Huang, Weimin

AU - Zhang, Zheling

AU - Han, Xiaojun

AU - Tang, Jilin

AU - Peng, Zhangquan

AU - Dong, Shaojun

AU - Wang, Erkang

PY - 2001/12/11

Y1 - 2001/12/11

N2 - The interaction of microperoxidase-11 (MP11) with cationic lipid vesicles of didodecyldimethylammonium bromide (DDAB) induces an α-helical conformation from random coil conformations in solution and this change then makes heme macrocycle more distorted. DDAB-induced MP11 conformations were investigated by cyclic votammetry (CV), circular dichroism (CD) and UV-vis spectrometry. All results indicate that the binding of MP11 in solution to DDAB vesicles and the ordered structure formation are driven by mostly electrostatic interaction between negatively charged residues in the undecapeptide and positively charged lipid headgroups on the membrane surface. Upon binding to DDAB, its half-peak potential was also changed. The mechanism of the interaction between MP11 and DDAB was also discussed.

AB - The interaction of microperoxidase-11 (MP11) with cationic lipid vesicles of didodecyldimethylammonium bromide (DDAB) induces an α-helical conformation from random coil conformations in solution and this change then makes heme macrocycle more distorted. DDAB-induced MP11 conformations were investigated by cyclic votammetry (CV), circular dichroism (CD) and UV-vis spectrometry. All results indicate that the binding of MP11 in solution to DDAB vesicles and the ordered structure formation are driven by mostly electrostatic interaction between negatively charged residues in the undecapeptide and positively charged lipid headgroups on the membrane surface. Upon binding to DDAB, its half-peak potential was also changed. The mechanism of the interaction between MP11 and DDAB was also discussed.

KW - Didodecyldimethylammonium bromide

KW - Electrochemistry

KW - Microperoxidase-11

KW - Spectroscopy

UR - https://www.scopus.com/pages/publications/0035846720

U2 - 10.1016/S0301-4622(01)00230-7

DO - 10.1016/S0301-4622(01)00230-7

M3 - 文章

C2 - 11744197

AN - SCOPUS:0035846720

SN - 0301-4622

VL - 94

SP - 165

EP - 173

JO - Biophysical Chemistry

JF - Biophysical Chemistry

IS - 1-2

ER -

Electrochemistry and spectroscopy study on the interaction of microperoxidase-11 with lipid membrane

Abstract

Keywords

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