Influence of head-group interactions on the miscibility of synthetic, stereochemically pure glycolipids and phospholipids [Erratum to document cited in CA109(3):19112d]

Biochemistry ◽  
1988 ◽  
Vol 27 (23) ◽  
pp. 8694-8694
Author(s):  
R. Koinova ◽  
H. L. Kuttenreich ◽  
B. Tenchov ◽  
H. J. Hinz
2011 ◽  
Vol 64 (6) ◽  
pp. 798 ◽  
Author(s):  
David I. Fernandez ◽  
Marc-Antoine Sani ◽  
Frances Separovic

The interactions of the antimicrobial peptide, maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH2) and two analogues, with model phospholipid membranes have been studied using solid-state NMR and circular dichroism spectroscopy. Maculatin 1.1 and the P15G and P15A analogues displayed minimal secondary structure in water, but with zwitterionic dimyristoylphosphatidylcholine (DMPC) vesicles displayed a significant increase in α-helical content. In mixed phospholipid vesicles of DMPC and anionic dimyristoylphosphatidylglycerol (DMPG), each peptide was highly structured with ~80% α-helical content. In DMPC vesicles, the native peptide displayed moderate head group interaction and significant perturbation of the lipid acyl chains. In DMPC/DMPG vesicles, maculatin 1.1 promoted formation of a DMPG-enriched phase and moderately increased disorder towards acyl chain ends of DMPC in the mixed bilayer. Both analogues showed reduced phospholipid head group interactions with DMPC but displayed significant interactions with the mixed lipid system. These effects support the preferential activity of these antimicrobial peptides for bacterial membranes.


2016 ◽  
Vol 18 (38) ◽  
pp. 26998-26998
Author(s):  
Sai J. Ganesan ◽  
Hongcheng Xu ◽  
Silvina Matysiak

Correction for ‘Effect of lipid head group interactions on membrane properties and membrane-induced cationic β-hairpin folding’ by Sai J. Ganesan et al., Phys. Chem. Chem. Phys., 2016, 18, 17836–17850.


1992 ◽  
Vol 96 (1) ◽  
pp. 446-452 ◽  
Author(s):  
Saima Kint ◽  
Paul H. Wermer ◽  
James R. Scherer

1996 ◽  
Vol 178 (1) ◽  
pp. 135-143 ◽  
Author(s):  
H. Baltes ◽  
M. Schwendler ◽  
C.A. Helm ◽  
H. Möhwald

RSC Advances ◽  
2014 ◽  
Vol 4 (61) ◽  
pp. 32579-32587 ◽  
Author(s):  
Subrata Chakraborty ◽  
Amitabha Chakraborty ◽  
Swapan K. Saha

The nature and size of strongly bound counter ions play crucial role in tuning the thermodynamics of micelle formation.


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