Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework (Q77080008)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11682479%20AND%20SRC:MED&resulttype=core&format=json

2 December 2019

title

Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework (English)

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2 December 2019

5

Robert E W Hancock

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2 December 2019

author name string

Leslie H Kondejewski

1

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2 December 2019

Darin L Lee

2

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2 December 2019

Masood Jelokhani-Niaraki

3

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2 December 2019

Susan W Farmer

4

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2 December 2019

Robert S Hodges

6

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2 December 2019

language of work or name

English

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publication date

26 October 2001

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Journal of Biological Chemistry

2 December 2019

published in

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2 December 2019

volume

277

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2 December 2019

issue

1

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2 December 2019

page(s)

67-74

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2 December 2019

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Nuclear Overhauser effect and cross-relaxation rate determinations of dihedral and transannular interproton distances in the decapeptide tyrocidine A.

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

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

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Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity.

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Environment-dependent conformation and antimicrobial activity of a gramicidin S analog containing leucine and lysine residues

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Unusual beta-sheet periodicity in small cyclic peptides

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Group additive contributions to the alcohol-induced alpha-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins.

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Identifiers

DOI

10.1074/JBC.M107825200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11682479%20AND%20SRC:MED&resulttype=core&format=json

2 December 2019

1 reference