The 2004 Biophysical Society-Avanti Award in Lipids address: roles of bilayer structure and elastic properties in peptide localization in membranes

McIntosh, Thomas J.

doi:10.1016/j.chemphyslip.2004.03.006

Cited by 25 publications

(19 citation statements)

References 98 publications

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“…Actually, some peptides that are very active in model membrane systems are much less active in the biological membrane system, and the contrary is also true. However, it should be noted that membrane systems having different lipid compositions have diverse properties which make them behave in significantly different ways (24). What is outstanding is that peptides 113 (ARDLICAQKFNGL TVL 828-843 ) and 123 (VLYENQKQIANQFNKAI 897-913 ) are located at the boundaries of R1, peptide 119 (GAALQIPFAMQM AYRF 873-888 ) is located inside R1, peptide 147 (FVFNGTSWFI TQRNFF 1077-1092 ) is located inside R2, and peptides 162 and 163 (LGKYEQYIKWPWYVWLGF 1185-1202 and KWPWYVWLG FIAGLIAIV 1193-1210 ) are located inside R3; all these regions represent surfaces with high bilayer-to-water transfer free-energy values (Fig.…”

Section: Discussionmentioning

confidence: 99%

Identification of the Membrane-Active Regions of the Severe Acute Respiratory Syndrome Coronavirus Spike Membrane Glycoprotein Using a 16/18-Mer Peptide Scan: Implications for the Viral Fusion Mechanism

Guillén

Pérez-Berná

Moreno

et al. 2005

J Virol

118

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We have identified the membrane-active regions of the severe acute respiratory syndrome coronavirus (SARS CoV) spike glycoprotein by determining the effect on model membrane integrity of a 16/18-mer SARS CoV spike glycoprotein peptide library. By monitoring the effect of this peptide library on membrane leakage in model membranes, we have identified three regions on the SARS CoV spike glycoprotein with membrane-interacting capabilities: region 1, located immediately upstream of heptad repeat 1 (HR1) and suggested to be the fusion peptide; region 2, located between HR1 and HR2, which would be analogous to the loop domain of human immunodeficiency virus type 1; and region 3, which would correspond to the pretransmembrane region. The identification of these membrane-active regions, which are capable of modifying the biophysical properties of phospholipid membranes, supports their direct role in SARS CoV-mediated membrane fusion, as well as facilitating the future development of SARS CoV entry inhibitors.

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Section: Discussionmentioning

confidence: 99%

Identification of the Membrane-Active Regions of the Severe Acute Respiratory Syndrome Coronavirus Spike Membrane Glycoprotein Using a 16/18-Mer Peptide Scan: Implications for the Viral Fusion Mechanism

Guillén

Pérez-Berná

Moreno

et al. 2005

J Virol

118

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“…5), the corresponding extracted ion chromatograms for doublyacylated melittin were understandably complex (see ESI). 5 Added to this, the retention times for some of the doubly acylated peptides overlapped those of the lyso-PCs, with potential effects on the magnitude of the ion currents observed. This made precise quantification of the extent of double acylation difficult.…”

Section: Minor Products In the Reaction With Popcmentioning

confidence: 99%

“…In particular, negtively charged lipids have been shown to enhance the membrane binding of melittin, 5 with the bound peptide exhibiting restricted conformational freedom when compared with PC membranes. Interestingly, with this lipid mixture, acyl transfer was only observed from 40 the PC component (Fig 8).…”

Section: 2-dioleoyl-3-phosphocholine (Dopc)/12-dipalmitoyl-3-phosmentioning

confidence: 99%

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The innate reactivity of a membrane associated peptide towards lipids: acyl transfer to melittin without enzyme catalysis

2012

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. (2012) 'The innate reactivity of a membrane associated peptide towards lipids : acyl transfer to melittin without enzyme catalysis.', Organic biomolecular chemistry., 10 (28). pp. 5371-5378.Further information on publisher's website:Publisher's copyright statement:Additional information: Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-prot purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details.

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“…The lipid membrane can be considered in a first approximation as a kind of special solvent that contributes to the stability and the folding of the particular polypeptides. The interaction of the peptides may be strongly dependent on the structural and elastic properties of the membrane (Hallock et al, 2002;McIntosh, 2004). Surfactant aggregates -reverse micelles (Hagen et al, 1990) and vesicles (Kuboi et al, 1997;Yoshimoto and Kuboi, 1999) -can function as "primitive chaperons" in the sense that they may catalyze the refolding of denatured proteins.…”

Section: Surfactant Aggregates As Folding and Reactivity Modifiers Ofmentioning

confidence: 99%

Surfactant Assemblies and their Various Possible Roles for the Origin(S) of Life

Walde

2006

Orig Life Evol Biosph

138

110

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A large number of surfactants (surface active molecules) are chemically simple compounds that can be obtained by simple chemical reactions, in some cases even under presumably prebiotic conditions. Surfactant assemblies are self-organized polymolecular aggregates of surfactants, in the simplest case micelles, vesicles, hexagonal and cubic phases. It may be that these different types of surfactant assemblies have played various, so-far underestimated important roles in the processes that led to the formation of the first living systems. Although nucleic acids are key players in the formation of cells as we know them today (RNA world hypothesis), it is still unclear how RNA could have been formed under prebiotic conditions. Surfactants with their self-organizing properties may have assisted, controlled and compartimentalized some of the chemical reactions that eventually led to the formation of molecules like RNA. Therefore, surfactants were possibly very important in prebiotic times in the sense that they may have been involved in different physical and chemical processes that finally led to a transformation of non-living matter to the first cellular form(s) of life. This hypothesis is based on four main experimental observations: (i) Surfactant aggregation can lead to cell-like compartimentation (vesicles). (ii) Surfactant assemblies can provide local reaction conditions that are very different from the bulk medium, which may lead to a dramatic change in the rate of chemical reactions and to a change in reaction product distributions. (iii) The surface properties of surfactant assemblies that may be liquid- or solid-like, charged or neutral, and the elasticity and packing density of surfactant assemblies depend on the chemical structure of the surfactants, on the presence of other molecules, and on the overall environmental conditions (e. g. temperature). This wide range of surface characteristics of surfactant assemblies may allow a control of surface-bound chemical reactions not only by the charge or hydrophobicity of the surface but also by its "softness". (iv) Chiral polymolecular assemblies (helices) may form from chiral surfactants. There are many examples that illustrate the different roles and potential roles of surfactant assemblies in different research areas outside of the field of the origin(s) of life, most importantly in investigations of contemporary living systems, in nanotechnology applications, and in the development of drug delivery systems. Concepts and ideas behind many of these applications may have relevance also in connection to the different unsolved problems in understanding the origin(s) of life.

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The 2004 Biophysical Society-Avanti Award in Lipids address: roles of bilayer structure and elastic properties in peptide localization in membranes

Cited by 25 publications

References 98 publications

Identification of the Membrane-Active Regions of the Severe Acute Respiratory Syndrome Coronavirus Spike Membrane Glycoprotein Using a 16/18-Mer Peptide Scan: Implications for the Viral Fusion Mechanism

Identification of the Membrane-Active Regions of the Severe Acute Respiratory Syndrome Coronavirus Spike Membrane Glycoprotein Using a 16/18-Mer Peptide Scan: Implications for the Viral Fusion Mechanism

The innate reactivity of a membrane associated peptide towards lipids: acyl transfer to melittin without enzyme catalysis

Surfactant Assemblies and their Various Possible Roles for the Origin(S) of Life

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