Side chain hydrophobicity modulates therapeutic activity and membrane selectivity of antimicrobial peptide mastoparan-X. (Q31153948)

1 September 2017

Side chain hydrophobicity modulates therapeutic activity and membrane selectivity of antimicrobial peptide mastoparan-X. (English)

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1 September 2017

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antimicrobial peptide

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4

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1 September 2017

Jonas R Henriksen

1

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Thomas Etzerodt

series ordinal

2

object named as

Thomas Etzerodt

1 reference

1 September 2017

Torben Gjetting

3

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PMC publication ID

3951324

1 September 2017

language of work or name

English

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publication date

12 March 2014

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1 September 2017

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1 September 2017

9

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1 September 2017

3

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1 September 2017

e91007

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Creative Commons Attribution 4.0 International

1 September 2017

start time

12 March 2014

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Selective acylation enhances membrane charge sensitivity of the antimicrobial peptide mastoparan-x.

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Peptide-liposome association. A critical examination with mastoparan-X.

21 June 2018

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21 June 2018

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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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Effects of L- or D-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic alpha-helical model peptide on structure and cell selectivity

21 January 2018

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21 January 2018

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Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation

21 January 2018

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Amphiphilic peptides in wasp venom

21 January 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/24621994

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Peptide binding to lipid bilayers. Binding isotherms and zeta-potential of a cyclic somatostatin analogue

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24621994

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/24621994

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1371/JOURNAL.PONE.0091007

1 reference

1 September 2017

0 references

1 reference

PMC publication ID

3951324

1 September 2017

PubMed publication ID

24621994

1 reference

PMC publication ID

3951324