Number and placement of hydrophobic residues in a longitudinal strip governs helix formation of peptides in the presence of lipid vesicles

S. Lu, T. Ciardelli, Victor Reyes, R. E. Humphreys

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

α-Helix formation of a peptidyl sequence is stabilized by hydrophobic residues recurring at positions which create a longitudinal hydrophobic strip upon folding of the sequence as a helix against a hydrophobic surface. To test that hypothesis, we measured by circular dichroism the helical coiling on lipid vesicles of nine analogs of a prototypic helix peptide PH-1.0, Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Thr-Gln-Thr-Leu-Lys. In these analogs, Thr was substituted for 1 or 2 Leu residues in the longitudinal hydrophobic strip Leu1...Leu5..Leu8...Leu12 which forms in the α-helical configuration. We found that coiling of analogs of Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Tyr-Gln-Thr-Leu-Lys on lipid vesicles depends upon the strength and structure of its longitudinal hydrophobic strip.

Original languageEnglish (US)
Pages (from-to)10054-10057
Number of pages4
JournalJournal of Biological Chemistry
Volume266
Issue number16
StatePublished - 1991
Externally publishedYes

Fingerprint

Lipids
Peptides
Circular Dichroism

ASJC Scopus subject areas

  • Biochemistry

Cite this

Number and placement of hydrophobic residues in a longitudinal strip governs helix formation of peptides in the presence of lipid vesicles. / Lu, S.; Ciardelli, T.; Reyes, Victor; Humphreys, R. E.

In: Journal of Biological Chemistry, Vol. 266, No. 16, 1991, p. 10054-10057.

Research output: Contribution to journalArticle

@article{f70787d4a85243a8b1fee545097d3b6f,
title = "Number and placement of hydrophobic residues in a longitudinal strip governs helix formation of peptides in the presence of lipid vesicles",
abstract = "α-Helix formation of a peptidyl sequence is stabilized by hydrophobic residues recurring at positions which create a longitudinal hydrophobic strip upon folding of the sequence as a helix against a hydrophobic surface. To test that hypothesis, we measured by circular dichroism the helical coiling on lipid vesicles of nine analogs of a prototypic helix peptide PH-1.0, Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Thr-Gln-Thr-Leu-Lys. In these analogs, Thr was substituted for 1 or 2 Leu residues in the longitudinal hydrophobic strip Leu1...Leu5..Leu8...Leu12 which forms in the α-helical configuration. We found that coiling of analogs of Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Tyr-Gln-Thr-Leu-Lys on lipid vesicles depends upon the strength and structure of its longitudinal hydrophobic strip.",
author = "S. Lu and T. Ciardelli and Victor Reyes and Humphreys, {R. E.}",
year = "1991",
language = "English (US)",
volume = "266",
pages = "10054--10057",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "16",

}

TY - JOUR

T1 - Number and placement of hydrophobic residues in a longitudinal strip governs helix formation of peptides in the presence of lipid vesicles

AU - Lu, S.

AU - Ciardelli, T.

AU - Reyes, Victor

AU - Humphreys, R. E.

PY - 1991

Y1 - 1991

N2 - α-Helix formation of a peptidyl sequence is stabilized by hydrophobic residues recurring at positions which create a longitudinal hydrophobic strip upon folding of the sequence as a helix against a hydrophobic surface. To test that hypothesis, we measured by circular dichroism the helical coiling on lipid vesicles of nine analogs of a prototypic helix peptide PH-1.0, Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Thr-Gln-Thr-Leu-Lys. In these analogs, Thr was substituted for 1 or 2 Leu residues in the longitudinal hydrophobic strip Leu1...Leu5..Leu8...Leu12 which forms in the α-helical configuration. We found that coiling of analogs of Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Tyr-Gln-Thr-Leu-Lys on lipid vesicles depends upon the strength and structure of its longitudinal hydrophobic strip.

AB - α-Helix formation of a peptidyl sequence is stabilized by hydrophobic residues recurring at positions which create a longitudinal hydrophobic strip upon folding of the sequence as a helix against a hydrophobic surface. To test that hypothesis, we measured by circular dichroism the helical coiling on lipid vesicles of nine analogs of a prototypic helix peptide PH-1.0, Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Thr-Gln-Thr-Leu-Lys. In these analogs, Thr was substituted for 1 or 2 Leu residues in the longitudinal hydrophobic strip Leu1...Leu5..Leu8...Leu12 which forms in the α-helical configuration. We found that coiling of analogs of Leu-Tyr-Gln-Glu-Leu-Gln-Lys-Leu-Tyr-Gln-Thr-Leu-Lys on lipid vesicles depends upon the strength and structure of its longitudinal hydrophobic strip.

UR - http://www.scopus.com/inward/record.url?scp=0025779077&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025779077&partnerID=8YFLogxK

M3 - Article

VL - 266

SP - 10054

EP - 10057

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 16

ER -