Liquid crystalline phases of hydrated phosphatidylethanolamine

Junger, E.; Reinauer, H.

doi:10.1016/0005-2736(69)90086-8

Cited by 54 publications

(12 citation statements)

References 8 publications

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“…Figure 3 shows how K11 affects also membranes mainly constituted by CL (CL 50% / POPC 50%). It should be noted that in the cases of CL and POPE, the addition of POPC was necessary for the formation of a MLV, due to their intrinsic shape and different T m [32,[62][63][64][65][66][67][68].…”

Section: K11 Selectivity Perturbs the Core Of Liposomes With Bacteriamentioning

confidence: 99%

Antimicrobial Peptide K11 Selectively Recognizes Bacterial Biomimetic Membranes and Acts by Twisting Their Bilayers

et al. 2020

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K11 is a synthetic peptide originating from the introduction of a lysine residue in position 11 within the sequence of a rationally designed antibacterial scaffold. Despite its remarkable antibacterial properties towards many ESKAPE bacteria and its optimal therapeutic index (320), a detailed description of its mechanism of action is missing. As most antimicrobial peptides act by destabilizing the membranes of the target organisms, we investigated the interaction of K11 with biomimetic membranes of various phospholipid compositions by liquid and solid-state NMR. Our data show that K11 can selectively destabilize bacterial biomimetic membranes and torque the surface of their bilayers. The same is observed for membranes containing other negatively charged phospholipids which might suggest additional biological activities. Molecular dynamic simulations reveal that K11 can penetrate the membrane in four steps: after binding to phosphate groups by means of the lysine residue at the N-terminus (anchoring), three couples of lysine residues act subsequently to exert a torque in the membrane (twisting) which allows the insertion of aromatic side chains at both termini (insertion) eventually leading to the flip of the amphipathic helix inside the bilayer core (helix flip and internalization).

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Section: K11 Selectivity Perturbs the Core Of Liposomes With Bacteriamentioning

confidence: 99%

Antimicrobial Peptide K11 Selectively Recognizes Bacterial Biomimetic Membranes and Acts by Twisting Their Bilayers

et al. 2020

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“…The thickness of the bilayer (=2Q) is -4 nm (41). The diameter of HI, rods in natural PE systems is 6-8 nm (3,(48)(49)(50). Using this diameter (7.0 nm) as the diameter of the inverted micelle (equals 2 rm) yields a diameter for the monolayer-enveloped structure of 11.0 nm.…”

Section: C I + -Ncmentioning

confidence: 99%

Inverted micellar structures in bilayer membranes. Formation rates and half-lives

Siegel¹

1984

Biophysical Journal

169

103

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Two sorts of inverted micellar structures have previously been proposed to explain morphological and 31P-NMR observations of bilayer systems. These structures only form in systems with components that can adopt the inverse hexagonal (HII) phase. LIP (lipidic particles) are intrabilayer structures, whereas IMI (inverted micellar intermediates) are structures that form between apposed bilayers. Here, we calculate the formation rates and half-lives of these structures to determine which (or if either) of these proposed structures is a likely explanation of the data. Calculations for the egg phosphatidylethanolamine and the Ca+-cardiolipin systems show that IMI form orders of magnitude faster than LIP, which should form slowly, if at all. This result is probably true in general, and indicates that "lipidic particle" electron micrograph images probably represent interbilayer structures, as some have previously proposed. It is shown here that IMI are likely intermediates in the lamellar----HII phase transitions and in the process of membrane fusion in some systems. The calculated formation rates, half-lives, and vesicle-vesicle fusion rates are in agreement with this observation.

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“…Their formation is favored by a high lysosomal content of phosphatidylethanolamine and of highly unsaturated fatty acids (126,177,178). Studies using in vitro models showed that the structural patterns of a phospholipid depend on the chemical nature of the PL, the presence of fusogenic lipids, the temperature and hydration (179,180). Increased hydration is associated with a loose packing of lamellae.…”

Section: Structural Types Of Myelinoid Bodiesmentioning

confidence: 99%

Pulmonary and generalized lysosomal storage induced by amphiphilic drugs.

Hruban¹

1984

Environ Health Perspect

105

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Administration of amphiphilic drugs to experimental animals causes formation of myelinoid bodies in many cell types, accumulation of foamy macrophages in pulmonary alveoli and pulmonary alveolar proteinosis. These changes are the result of an interaction between the drugs and phospholipids which leads to an alteration in physicochemical properties of the phospholipids. Impairment of the digestion of altered pulmonary secretions in phagosomes of macrophages results in accumulation of foam cells in pulmonary alveoli. Impairment of the metabolism of altered phospholipids removed by autophagy induces an accumulation of myelinoid bodies. The administration of amphiphilic compounds thus causes pulmonary intra-alveolar histiocytosis which is a part of a drug-induced lysosomal storage or generalized lipidosis. The accumulation of drug-lipid complexes in myelinoid bodies and in pulmonary foam cells may lead to alteration of cellular functioning and to clinical disease. Currently over 50 amphiphilic drugs are known. Unique pharmacological properties necessitate clinical use of some of these drugs. The occurrence and severity of potential clinical side effects depend on the nature of each drug, dosage and duration of treatment, simultaneous administration of other drugs and foods, individual metabolic pattern of the patient and other factors. Further studies on factors preventing and potentiating adverse effects of amphiphilic drugs are indicated.ImagesFIGURE 1.FIGURE 2.FIGURE 3.FIGURE 4.FIGURE 5.FIGURE 6.FIGURE 7.FIGURE 8.FIGURE 9.FIGURE 10.

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Liquid crystalline phases of hydrated phosphatidylethanolamine

Cited by 54 publications

References 8 publications

Antimicrobial Peptide K11 Selectively Recognizes Bacterial Biomimetic Membranes and Acts by Twisting Their Bilayers

Antimicrobial Peptide K11 Selectively Recognizes Bacterial Biomimetic Membranes and Acts by Twisting Their Bilayers

Inverted micellar structures in bilayer membranes. Formation rates and half-lives

Pulmonary and generalized lysosomal storage induced by amphiphilic drugs.

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