(Q57362685)

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Ideally amphipathic β-sheeted peptides at interfaces: structure, orientation, affinities for lipids and hemolytic activity of (KL)mK peptides

scientific article published on 01 January 2000

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10631295%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

Ideally amphipathic beta-sheeted peptides at interfaces: structure, orientation, affinities for lipids and hemolytic activity of (KL)(m)K peptides (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10631295%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

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S Castano

1

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3 November 2019

B Desbat

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10631295%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

J Dufourcq

3

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3 November 2019

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1 January 2000

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3 November 2019

Biochimica et Biophysica Acta

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3 November 2019

1463

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3 November 2019

1

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3 November 2019

65-80

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3 November 2019

Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities

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The amphipathic helix concept: length effects on ideally amphipathic LiKj(i=2j) peptides to acquire optimal hemolytic activity

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Design of model amphipathic peptides having potent antimicrobial activities

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Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes.

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

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Are interactions with phospholipids responsible for pharmacological activities of cardiotoxins?

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Defensins: endogenous antibiotic peptides of animal cells

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Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization

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The secondary structure of the insect defensin A depends on its environment. A circular dichroism study

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Role of disulfide linkages in tachyplesin-lipid interactions.

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Synthesis and solution structure of the antimicrobial peptide protegrin-1.

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Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analog

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Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin

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Penetration of the insect defensin A into phospholipid monolayers and formation of defensin A-lipid complexes

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Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs

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Design and synthesis of basic peptides having amphipathic β-structure and their interaction with phospholipid membranes

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Polyalanine-based peptides as models for self-associated beta-pleated-sheet complexes

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7 January 2021

Folding of beta-sheet membrane proteins: a hydrophobic hexapeptide model

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7 January 2021

Conformation of a water-soluble beta-sheet model peptide. A circular dichroism and Fourier-transform infrared spectroscopic study of double D-amino acid replacements.

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7 January 2021

Induced conformational states of amphipathic peptides in aqueous/lipid environments

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7 January 2021

In situ study by polarization modulated Fourier transform infrared spectroscopy of the structure and orientation of lipids and amphipathic peptides at the air-water interface

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7 January 2021

Formation of stable polypeptide monolayers at interfaces: controlling molecular conformation and orientation

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7 January 2021

The amphipathic alpha-helix concept. Application to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin

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7 January 2021

Structural characterisation of the natural membrane-bound state of melittin: a fluorescence study of a dansylated analogue

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7 January 2021

Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles

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Nanosecond fluorescence spectroscopy of macromolecules

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The helical hydrophobic moment: a measure of the amphiphilicity of a helix

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Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin

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Identifiers

10.1016/S0005-2736(99)00175-3

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10631295%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10631295%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

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