Chemically Reactive Derivatives of Gramicidin A for Developing Ion Channel-Based Nanoprobes

2008 ◽  
Vol 19 (8) ◽  
pp. 1614-1624 ◽  
Author(s):  
Steven Blake ◽  
Ricardo Capone ◽  
Michael Mayer ◽  
Jerry Yang
Keyword(s):  
Ion Channel ◽  
Gramicidin A ◽  
Derivatives Of

scholarly journals Redox-regulated ion channel activity of a cysteine-containing gramicidin A analogue

2006 ◽  
Vol 1758 (4) ◽  
pp. 493-498 ◽  
Author(s):  
Yuri N. Antonenko ◽  
Tatyana B. Stoilova ◽  
Sergey I. Kovalchuk ◽  
Natalya S. Egorova ◽  
Alina A. Pashkovskaya ◽  
...  
Keyword(s):  
Ion Channel ◽  
Gramicidin A ◽  
Channel Activity

An asymmetric ion channel derived from gramicidin A

FEBS Journal ◽  
2005 ◽  
Vol 272 (4) ◽  
pp. 975-986 ◽  
Author(s):  
Xiulan Xie ◽  
Lo'ay Al-Momani ◽  
Philipp Reiß ◽  
Christian Griesinger ◽  
Ulrich Koert
Keyword(s):  
Ion Channel ◽  
Gramicidin A

The divalent cation-binding sites of gramicidin A transmembrane ion-channel

Biopolymers ◽  
1991 ◽  
Vol 31 (4) ◽  
pp. 425-434 ◽  
Author(s):  
A. P. Golovanov ◽  
I. L. Barsukov ◽  
A. S. Arseniev ◽  
V. F. Bystrov ◽  
S. V. Sukhanov ◽  
...  
Keyword(s):  
Ion Channel ◽  
Divalent Cation ◽  
Binding Sites ◽  
Cation Binding ◽  
Gramicidin A

scholarly journals Discovery of gramicidin A analogues with altered activities by multidimensional screening of a one-bead-one-compound library

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Yuri Takada ◽  
Hiroaki Itoh ◽  
Atmika Paudel ◽  
Suresh Panthee ◽  
Hiroshi Hamamoto ◽  
...  
Keyword(s):  
Ion Channel ◽  
Large Scale ◽  
Antibacterial Activities ◽  
Gramicidin A ◽  
Ion Concentration ◽  
Peptide Antibiotic ◽  
Structure Activity ◽  
Common Ion ◽  
Multidimensional Screening ◽  
The Common

Abstract Gramicidin A (1) is a peptide antibiotic that disrupts the transmembrane ion concentration gradient by forming an ion channel in a lipid bilayer. Although long used clinically, it is limited to topical application because of its strong hemolytic activity and mammalian cytotoxicity, likely arising from the common ion transport mechanism. Here we report an integrated high-throughput strategy for discovering analogues of 1 with altered biological activity profiles. The 4096 analogue structures are designed to maintain the charge-neutral, hydrophobic, and channel forming properties of 1. Synthesis of the analogues, tandem mass spectrometry sequencing, and 3 microscale screenings enable us to identify 10 representative analogues. Re-synthesis and detailed functional evaluations find that all 10 analogues share a similar ion channel function, but have different cytotoxic, hemolytic, and antibacterial activities. Our large-scale structure-activity relationship studies reveal the feasibility of developing analogues of 1 that selectively induce toxicity toward target organisms.

scholarly journals Density-functional theory study of gramicidin A ion channel geometry and electronic properties

2013 ◽  
Vol 10 (89) ◽  
pp. 20130547 ◽  
Author(s):  
Milica Todorović ◽  
David R. Bowler ◽  
Michael J. Gillan ◽  
Tsuyoshi Miyazaki
Keyword(s):  
Amino Acids ◽  
Density Functional Theory ◽  
Ion Channel ◽  
Ground State ◽  
Density Functional ◽  
Gramicidin A ◽  
Linear Scaling ◽  
Side Chains ◽  
Functional Theory ◽  
Ground State Geometry

Understanding the mechanisms underlying ion channel function from the atomic-scale requires accurate ab initio modelling as well as careful experiments. Here, we present a density functional theory (DFT) study of the ion channel gramicidin A (gA), whose inner pore conducts only monovalent cations and whose conductance has been shown to depend on the side chains of the amino acids in the channel. We investigate the ground state geometry and electronic properties of the channel in vacuum, focusing on their dependence on the side chains of the amino acids. We find that the side chains affect the ground state geometry, while the electrostatic potential of the pore is independent of the side chains. This study is also in preparation for a full, linear scaling DFT study of gA in a lipid bilayer with surrounding water. We demonstrate that linear scaling DFT methods can accurately model the system with reasonable computational cost. Linear scaling DFT allows ab initio calculations with 10 000–100 000 atoms and beyond, and will be an important new tool for biomolecular simulations.

scholarly journals Ion Channel Regulation by Lipid Bilayers: Theory & Simulation of Deformed Membranes around Gramicidin A

2015 ◽  
Vol 108 (2) ◽  
pp. 209a ◽  
Author(s):  
Andrew H. Beaven ◽  
Alexander J. Sodt ◽  
Olaf S. Andersen ◽  
Richard W. Pastor ◽  
Wonpil Im
Keyword(s):  
Ion Channel ◽  
Lipid Bilayers ◽  
Gramicidin A ◽  
Ion Channel Regulation ◽  
Channel Regulation
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