The tryptophans of gramicidin are essential for the lipid structure modulating effect of the peptide.

Biochimica et biophysica acta ·Vol. 820 ·No. 1 ·1985-10-24 ·Pages 154-6

Killian JA, Timmermans JW, Keur S, de Kruijff B

Abstract

It is shown that N-formylation of the tryptophan residues of gramicidin completely and reversibly blocks the hexagonal HII phase-inducing ability of the peptide in dioleoylphosphatidylcholine model membranes.

MeSH Terms

Amino Acid Sequence Chemical Phenomena Chemistry Formates Gramicidin/pharmacology Lipid Bilayers Liposomes Magnetic Resonance Spectroscopy Membrane Lipids/physiology Phosphatidylcholines Structure-Activity Relationship Tryptophan

Chemicals

Formates Lipid Bilayers Liposomes Membrane Lipids Phosphatidylcholines formic acid Gramicidin Tryptophan 1,2-oleoylphosphatidylcholine

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Killian J A

Timmermans J W

Keur S

de Kruijff B

Article Info

Journal

Biochimica et biophysica acta

Abbr.

Biochim Biophys Acta

ISSN

0006-3002

DOI

10.1016/0005-2736(85)90227-5

Published

1985-10-24

Pages

154-6

Language

English

Region

Netherlands

NLM ID

0217513

Subset

External Links

PubMed source DOI: 10.1016/0005-2736(85)90227-5

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The tryptophans of gramicidin are essential for the lipid structure modulating effect of the peptide.

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