Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment. (Q52997907)

10 May 2018

title

Modulation of membrane activity of amphipathic, antibacterial peptides by slight modifications of the hydrophobic moment. (English)

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10 May 2018

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Wieprecht T

1

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10 May 2018

Dathe M

2

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10 May 2018

Krause E

3

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10 May 2018

Beyermann M

4

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10 May 2018

Maloy WL

5

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MacDonald DL

6

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10 May 2018

Bienert M

7

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10 May 2018

language of work or name

English

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publication date

1 November 1997

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10 May 2018

published in

FEBS Letters

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10 May 2018

volume

417

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issue

1

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10 May 2018

page(s)

135-140

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10 May 2018

Design of model amphipathic peptides having potent antimicrobial activities

cites work

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Augmentation of the antibacterial activity of magainin by positive-charge chain extension

21 January 2018

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

21 January 2018

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Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes.

21 January 2018

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Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides.

21 January 2018

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Three-dimensional structure of membrane and surface proteins

21 January 2018

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Structure-function studies of amphiphilic antibacterial peptides.

21 January 2018

1 reference

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Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion

21 January 2018

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Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles.

21 January 2018

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Diastereoisomers of cytolysins, a novel class of potent antibacterial peptides

21 January 2018

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Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy

21 January 2018

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Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2.

21 January 2018

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Production of large unilamellar vesicles by a rapid extrusion procedure: characterization of size distribution, trapped volume and ability to maintain a membrane potential

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21 January 2018

https://api.crossref.org/works/10.1016%2FS0014-5793%2897%2901266-0

inferred from DOI database lookup

7 January 2021

based on heuristic

Relationship between antimicrobial activity and amphiphilic property of basic model peptides

1 reference

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Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides

21 January 2018

1 reference

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Design and synthesis of amphiphilic alpha-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes

21 January 2018

1 reference

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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

21 January 2018

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Design and synthesis of amphipathic antimicrobial peptides

21 January 2018

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A rapid and sensitive sub-micro phosphorus determination

21 January 2018

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Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer

21 January 2018

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Membrane partition coefficients chromatographically measured using immobilized artificial membrane surfaces

21 January 2018

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Synthetic magainin analogues with improved antimicrobial activity

21 January 2018

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Influence of tryptophan residues on melittin's hemolytic activity

21 January 2018

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Conformational and functional study of magainin 2 in model membrane environments using the new approach of systematic double-D-amino acid replacement

21 January 2018

1 reference

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10.1016/S0014-5793(97)01266-0

21 January 2018

Identifiers

DOI

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10 May 2018

PubMed ID

9395091

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10 May 2018