Antimicrobial peptides stand as promising therapeutics to mitigate the global rise of antibiotic resistance. They generally act by perturbing the bacterial cell membrane, and are thus less likely to induce resistance. Since they are membrane-active molecules, it is critical to verify and understand their potential action towards eukaryotic cells to help design effective and safe drugs. In this work, we studied the interaction of two antimicrobial peptides, aurein 1.2 and caerin 1.1, with red...
[NMR paper] Solution and solid-state NMR structural investigations of the antimicrobial designer peptide GL13K in membranes.
Solution and solid-state NMR structural investigations of the antimicrobial designer peptide GL13K in membranes.
Related Articles Solution and solid-state NMR structural investigations of the antimicrobial designer peptide GL13K in membranes.
Biochemistry. 2017 Jul 12;:
Authors: Harmouche N, Aisenbrey C, Porcelli F, Xia Y, Nelson SED, Chen X, Raya J, Vermeer LS, Aparicio C, Veglia G, Gorr SU, Bechinger B
Abstract
The antimicrobial peptide GL13K encompasses 13 amino acid residues and has been designed and optimized from the...
nmrlearner
Journal club
0
07-13-2017 12:02 PM
Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR
Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR
Publication date: December 2016
Source:Biochimica et Biophysica Acta (BBA) - Bioenergetics, Volume 1857, Issue 12</br>
Author(s): Fatemeh Azadi Chegeni, Giorgio Perin, Karthick Babu Sai Sankar Gupta, Diana Simionato, Tomas Morosinotto, Anjali Pandit</br>
Photosynthetic thylakoid membranes contain the protein machinery to convert sunlight in chemical energy and regulate this process in changing environmental conditions via interplay between lipid,...
nmrlearner
Journal club
0
09-22-2016 06:33 AM
[NMR paper] Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein and lipid dynamics in photosynthetic thylakoid membranes investigated by in-situ solid-state NMR.
Biochim Biophys Acta. 2016 Sep 11;
Authors: Chegeni FA, Perin G, Gupta KB, Simionato D, Morosinotto T, Pandit A
Abstract
Photosynthetic thylakoid membranes contain the protein...
nmrlearner
Journal club
0
09-22-2016 06:31 AM
[NMR paper] A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles A 2H solid-state NMR study of lipid clustering by cationic antimicrobial and cell-penetrating peptides in model bacterial membranes.
Biophys J. 2013 Nov 19;105(10):2333-42
Authors: Kwon B, Waring AJ, Hong M
Abstract
Domain formation in bacteria-mimetic membranes...
nmrlearner
Journal club
0
07-12-2014 04:28 AM
[NMR paper] Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study.
Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study.
Related Articles Interactions of lipopolysaccharide with lipid membranes, raft models - a solid state NMR study.
Biochim Biophys Acta. 2013 Apr 5;
Authors: Ciesielski F, Griffin DC, Rittig M, Moriyón I, Bonev BB
Abstract
Lipopolysaccharide (LPS) is a major component of the external leaflet of bacterial outer membranes, key pro-inflammatory factor and an important mediator of host-pathogen interactions. In host cells it activates the complement...
nmrlearner
Journal club
0
04-10-2013 07:21 PM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
Riqiang Fu, Xingsheng Wang, Conggang Li, Adriana N. Santiago-Miranda, Gary J. Pielak and Fang Tian
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja204062v/aop/images/medium/ja-2011-04062v_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja204062v
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/BuOPwKpaHdw
nmrlearner
Journal club
0
07-27-2011 11:24 AM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
J Am Chem Soc. 2011 Jul 21;
Authors: Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F
The feasibility of using solid state MAS NMR for in situ structural characterization of the LR11 (sorLA) transmembrane domain in native Escherichia coli (E. coli) membranes is presented. LR11 interacts with...
nmrlearner
Journal club
0
07-23-2011 08:54 AM
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes fro
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
Related Articles 19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
J Am Chem Soc. 2010 Jul 7;132(26):8822-4
Authors: Ieronimo M, Afonin S, Koch K, Berditsch M, Wadhwani P, Ulrich AS
(19)F NMR is a unique tool to examine the structure of fluorine-labeled peptides in their native cellular environment, due to an exquisite sensitivity...
IN SITU SOLID-STATE NMR STUDY OF ANTIMICROBIAL PEPTIDE INTERACTIONs WITH ERYTHROCYTE MEMBRANES
Linear Mode
