Synthesis of Amphiphilic Helix–Coil–Helix Poly(3-(glycerylthio)propyl isocyanate)-block-polystyrene-block-poly(3-(glycerylthio)propyl isocyanate)

2018 ◽  
Vol 51 (3) ◽  
pp. 697-704 ◽  
Author(s):  
Chang-Geun Chae ◽  
Ho-Bin Seo ◽  
In-Gyu Bak ◽  
Jae-Suk Lee
2021 ◽  
Vol 7 (4) ◽  
pp. 1475-1484
Author(s):  
Kayo Terada ◽  
Joan Gimenez-Dejoz ◽  
Taichi Kurita ◽  
Kazusato Oikawa ◽  
Hirotaka Uji ◽  
...  

Author(s):  
Tse-Lok Ho ◽  
Mary Fieser ◽  
Louis Fieser
Keyword(s):  

2001 ◽  
Vol 67 (4) ◽  
pp. 1418-1422 ◽  
Author(s):  
C. Corbier ◽  
F. Krier ◽  
G. Mulliert ◽  
B. Vitoux ◽  
A.-M. Revol-Junelles

ABSTRACT The antibacterial spectra and modes of action of synthetic peptides corresponding to mesenterocin 52B and leucocin B-TA33a greatly differ despite their high sequence homology. Circular dichroism experiments establish the capacity of each of these two peptides to partly fold into an amphiphilic helix that might be crucial for their adsorption at lipophilic-hydrophilic interfaces.


2017 ◽  
Author(s):  
Zhen-lu Li

AbstractThe N-terminal amphiphilic helices of proteins Epsin, Sar1p and Arf1 play a critical role in initiating membrane deformation. We present here the study of the interactions of these amphiphilic helices with the lipid membranes by combining the all-atom and coarse-grained simulations. In the all-atom simulations, we find that the amphiphilic helices of Epsin and Sar1p have a shallower insertion depth into the membrane compared to the amphiphilic helix of Arf1, but remarkably, the amphiphilic helices of Epsin and Sar1p induce higher asymmetry in the lipid packing between the two monolayers of the membrane. The insertion depth of amphiphilic helix into the membrane is determined not only by the overall hydrophobicity but also by the specific distribution of polar and non-polar residues along the helix. To directly compare their ability of deforming the membrane, we further apply coarse-grained simulations to investigate the membranes deformation under the insertion of multiple helices. Importantly, it is found that the amphiphilic helices of Epsin and Sar1p generate a larger membrane curvature than that of Arf1, in accord with the experimental results qualitatively. These findings enhance our understanding of the molecular mechanism of the protein-driven membrane remodeling.


Peptides ◽  
1992 ◽  
pp. 37-39
Author(s):  
H. Gordon ◽  
W. Neugebauer ◽  
R. Rixon ◽  
R. Somorjai ◽  
W. Sung ◽  
...  

2011 ◽  
Vol 437 (3) ◽  
pp. 389-397 ◽  
Author(s):  
Bastian Thaa ◽  
Ilya Levental ◽  
Andreas Herrmann ◽  
Michael Veit

The influenza virus transmembrane protein M2 is a proton channel, but also plays a role in the scission of nascent virus particles from the plasma membrane. An amphiphilic helix in the CT (cytoplasmic tail) of M2 is supposed to insert into the lipid bilayer, thereby inducing curvature. Palmitoylation of the helix and binding to cholesterol via putative CRAC (cholesterol recognition/interaction amino acid consensus) motifs are believed to target M2 to the edge of rafts, the viral-budding site. In the present study, we tested pre-conditions of this model, i.e. that the CT interacts with membranes, and that acylation and cholesterol binding affect targeting of M2. M2-CT, purified as a glutathione transferase fusion protein, associated with [3H]photocholesterol and with liposomes. Mutation of tyrosine residues in the CRAC motifs prevented [3H]photocholesterol labelling and reduced liposome binding. M2-CT fused to the yellow fluorescent protein localized to the Golgi in transfected cells; membrane targeting was dependent on CRAC and (to a lesser extent) on palmitoylation. Preparation of giant plasma membrane vesicles from cells expressing full-length M2–GFP (green fluorescent protein) showed that the protein is partly present in the raft domain. Raft targeting required palmitoylation, but not the CRAC motifs. Thus palmitoylation and cholesterol binding differentially affect the intrinsic membrane binding of the amphiphilic helix.


2012 ◽  
Vol 1818 (12) ◽  
pp. 3025-3031 ◽  
Author(s):  
Marco J. Klein ◽  
Stephan L. Grage ◽  
Claudia Muhle-Goll ◽  
Jochen Bürck ◽  
Sergii Afonin ◽  
...  

1992 ◽  
Vol 27 (6) ◽  
pp. 591-597 ◽  
Author(s):  
Jeffrey W. Gilman ◽  
Yoshiko A. Otonari ◽  
Robert D. Chapman
Keyword(s):  

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