Effect of salts on conformational change of basic amphipathic peptides from β-structure to α-helix in the presence of phospholipid liposomes and their channel-forming ability

1993 ◽  
Vol 1151 (1) ◽  
pp. 76-82 ◽  
Author(s):  
Sannamu Lee ◽  
Toshihide Iwata ◽  
Hatsuyo Oyagi ◽  
Haruhiko Aoyagi ◽  
Motonori Ohno ◽  
...  
Keyword(s):  
Conformational Change ◽  
Amphipathic Peptides ◽  
Phospholipid Liposomes ◽  
Α Helix

α-Helix to β-sheet transition within the Leu i Lys j (i=2j) series of lytic amphipathic peptides by decreasing their size

1997 ◽  
Vol 4 (4-6) ◽  
pp. 195-200 ◽  
Author(s):  
Sabine Castano ◽  
Bernard Desbat ◽  
Isabelle Cornut ◽  
Philippe Méléard ◽  
Jean Dufourcq
Keyword(s):  
Amphipathic Peptides ◽  
Α Helix ◽  
Β Sheet

scholarly journals Lysenin toxin insertion mechanism is Calcium-dependent

2019 ◽  
Author(s):  
Ignacio L.B. Munguira
Keyword(s):  
Conformational Change ◽  
Virulence Factors ◽  
Calcium Ions ◽  
Calcium Sensitivity ◽  
Triggering Mechanism ◽  
Calcium Dependent ◽  
Insertion Mechanism ◽  
Ph Decrease ◽  
Α Helix ◽  
Structural Descriptions

AbstractPore Forming Toxins (PFTs), formed mainly by virulence factors of bacteria, belongs to Pore Forming Protein (PFP) family. Secreted as soluble monomers, they bind specific targets in membranes where their oligomerization and insertion place. Lysenin, a member of the PFTs, forms and oligomer after sphingomyelin binding, the so-called prepore, which become inserted forming a pore after a conformational change triggered by a pH decrease. In crowded conditions, oligomers tends to stay in prepore form because the prepore-to-pore transition is sterically blocked. In this study, we investigate the effect of calcium ions in those crowded conditions, finding that calcium act as a trigger for lysenin insertion. We localize the residues responsible for calcium sensitivity in a small α-helix. Our results are not only one of the few complete structural descriptions of prepore-to-pore transitions but the very first that involves a calcium triggering mechanism. The presence of glutamic or aspartic acids in the insertion domains could be an indication that calcium may be a general trigger for PFTs and more generally PFP.

Helical α/β-depsipeptides with alternating residue types: conformational change from the 11-helix to the 14/15-helix

2016 ◽  
Vol 14 (36) ◽  
pp. 8438-8442 ◽  
Author(s):  
Jaeyeon Lee ◽  
Geunhyeok Jang ◽  
Philjae Kang ◽  
Moon-Gun Choi ◽  
Soo Hyuk Choi
Keyword(s):  
Lactic Acid ◽  
Conformational Change ◽  
The Third ◽  
N Terminus ◽  
Α Helix

Short α/β-depsipeptides of which the third residue from the N-terminus is an (S)-lactic acid residue predominantly adopt 14/15-helical conformations analogous to the α-helix.

Phosphatidylserine-selective Conformational Change of α-Helix Peptide, Td3717, and Its Ability to Transfect Cancer Cells

2009 ◽  
Vol 38 (7) ◽  
pp. 684-685 ◽  
Author(s):  
Shinichi Kuriyama ◽  
Kanako Nishimura ◽  
Yasushi Taguchi ◽  
Kazutoshi Yanagibashi ◽  
Yoshiki Katayama ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Conformational Change ◽  
Α Helix

Pro-apoptotic bax-α1 synthesis and evidence for β-sheet to α-helix conformational change as triggered by negatively charged lipid membranes

2007 ◽  
Vol 13 (2) ◽  
pp. 100-106 ◽  
Author(s):  
Marc-Antoine Sani ◽  
Cécile Loudet ◽  
Gerhard Gröbner ◽  
Erick J. Dufourc
Keyword(s):  
Conformational Change ◽  
Lipid Membranes ◽  
Α Helix ◽  
Β Sheet

Solvent Effects on the 310-/α-Helix Equilibrium in Short Amphipathic Peptides Rich in α,α-Disubstituted Amino Acids

1997 ◽  
Vol 119 (5) ◽  
pp. 1167-1168 ◽  
Author(s):  
T. Scott Yokum ◽  
Ted J. Gauthier ◽  
Robert P. Hammer ◽  
Mark L. McLaughlin
Keyword(s):  
Amino Acids ◽  
Solvent Effects ◽  
Amphipathic Peptides ◽  
Α Helix ◽  
Disubstituted Amino Acids

scholarly journals Membrane-induced conformational change in human apolipoprotein H

2000 ◽  
Vol 348 (1) ◽  
pp. 103-106 ◽  
Author(s):  
Shao-Xiong WANG ◽  
Yu-Tong SUN ◽  
Sen-Fang SUI
Keyword(s):  
Conformational Change ◽  
Lipid Membrane ◽  
Membrane Surface ◽  
Basic Mechanism ◽  
Cd Spectroscopy ◽  
Model Systems ◽  
Anionic Phospholipid ◽  
Human Apolipoprotein ◽  
Apolipoprotein H ◽  
Α Helix

The interaction of apolipoprotein H (Apo H) with lipid membrane has been considered to be a basic mechanism for the biological function of the protein. Previous reports have demonstrated that Apo H can interact only with membranes containing anionic phospholipids. Here we study the membrane-induced conformational change of Apo H by CD spectroscopy with two different model systems: anionic-phospholipid-containing liposomes [such as 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) and cardiolipin], and the water/methanol mixtures at moderately low pH, which mimic the micro-physicochemical environment near the membrane surface. It is found that Apo H undergoes a remarkable conformational change on interaction with liposomes containing anionic phospholipid. To interact with liposomes containing DMPG, there is a 6.8% increase in α-helix in the secondary structures; in liposomes containing cardiolipin, however, there is a 12.6% increase in α-helix and a 9% decrease in β-sheet. The similar conformation change in Apo H can be induced by treatment with an appropriate mixture of water/methanol. The results indicate that the association of Apo H with membrane is correlated with a certain conformational change in the secondary structure of the protein.

scholarly journals Gating the pore of the calcium-activated chloride channel TMEM16A

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Andy K. M. Lam ◽  
Jan Rheinberger ◽  
Cristina Paulino ◽  
Raimund Dutzler
Keyword(s):  
Electron Microscopy ◽  
Conformational Change ◽  
Physical Contact ◽  
Open Probability ◽  
Hydrophobic Residues ◽  
Closed Conformation ◽  
Basal Activity ◽  
Cryo Electron Microscopy ◽  
Selective Channel ◽  
Α Helix

AbstractThe binding of cytoplasmic Ca2+ to the anion-selective channel TMEM16A triggers a conformational change around its binding site that is coupled to the release of a gate at the constricted neck of an hourglass-shaped pore. By combining mutagenesis, electrophysiology, and cryo-electron microscopy, we identified three hydrophobic residues at the intracellular entrance of the neck as constituents of this gate. Mutation of each of these residues increases the potency of Ca2+ and results in pronounced basal activity. The structure of an activating mutant shows a conformational change of an α-helix that contributes to Ca2+ binding as a likely cause for the basal activity. Although not in physical contact, the three residues are functionally coupled to collectively contribute to the stabilization of the gate in the closed conformation of the pore, thus explaining the low open probability of the channel in the absence of Ca2+.

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