|
|
|
|
| LEADER |
01000caa a22002652 4500 |
| 001 |
NLM298112531 |
| 003 |
DE-627 |
| 005 |
20250225112734.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231225s2019 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1021/acs.langmuir.9b01251
|2 doi
|
| 028 |
5 |
2 |
|a pubmed25n0993.xml
|
| 035 |
|
|
|a (DE-627)NLM298112531
|
| 035 |
|
|
|a (NLM)31194562
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Su, ZhangFei
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a In Situ Electrochemical and PM-IRRAS Studies of Colicin E1 Ion Channels in the Floating Bilayer Lipid Membrane
|
| 264 |
|
1 |
|c 2019
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 17.08.2020
|
| 500 |
|
|
|a Date Revised 17.08.2020
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a Colicin E1 is a channel-forming bacteriocin produced by certain Escherichia coli cells in an effort to reduce competition from other bacterial strains. The colicin E1 channel domain was incorporated into a 1,2-diphytanoyl- sn-glycero-3-phosphocholine floating bilayer situated on a 1-thio-?-d-glucose-modified gold (111) surface. The electrochemical properties of the colicin E1 channel in the floating bilayer were measured by electrochemical impedance spectroscopy; the configuration and orientation of colicin E1 in the bilayer were determined by polarization-modulation-infrared-reflection absorption spectroscopy. The EIS and IR results indicate that colicin E1 adopts a closed-channel state at the positive transmembrane potential, leading to high membrane resistance and a large tilt angle of ?-helices. When the transmembrane potential becomes negative, colicin E1 begins to insert into the lipid bilayer, corresponding to low membrane resistance and a low tilt angle of ?-helices. The insertion of colicin E1 into the lipid bilayer is driven by the negative transmembrane potential, and the ion-channel open and closed states are potential reversible. The data in this report provide new insights into the voltage-gated mechanism of colicin E1 ion channels in phospholipid bilayers and illustrate that the floating bilayer lipid membrane at the metal electrode surface is a robust platform to study membrane-active proteins and peptides in a quasi-natural environment
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Research Support, Non-U.S. Gov't
|
| 650 |
|
7 |
|a Colicins
|2 NLM
|
| 650 |
|
7 |
|a Ion Channels
|2 NLM
|
| 650 |
|
7 |
|a Lipid Bilayers
|2 NLM
|
| 700 |
1 |
|
|a Ho, Derek
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Merrill, A Rod
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Lipkowski, Jacek
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 35(2019), 25 vom: 25. Juni, Seite 8452-8459
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
|
| 773 |
1 |
8 |
|g volume:35
|g year:2019
|g number:25
|g day:25
|g month:06
|g pages:8452-8459
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1021/acs.langmuir.9b01251
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_22
|
| 912 |
|
|
|a GBV_ILN_350
|
| 912 |
|
|
|a GBV_ILN_721
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 35
|j 2019
|e 25
|b 25
|c 06
|h 8452-8459
|