Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles

Rickey Paige Hicks, Erin Mones, Hanah Kim, Brandon W. Koser, Daniel A. Nichols, Apurba K. Bhattacharjee

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

The role played by noncovalent interactions in inducing a stable secondary structure onto the sodium dodecyl sulfate (SDS) and dodecylphosphocholine (DPC) micelle-bound conformations of (Ala8,13,18)magainin 2 amide and the DPC micelle bound conformation of magainin 1 were determined. Two-dimensional NMR and molecular modeling investigations indicated that (Ala8,13,18)magainin 2 amide bound to DPC micelles adopts a α-helical secondary structure involving residues 2-16. The four C-terminal residues converge to a lose β-turn structure. (Ala8,13,18)magainin 2 amide bound to SDS miscelles adopts a α-helical secondary structure involving residues 7-18. The C- and N-terminal residues exhibited a great deal of conformational flexibility. Magainin 1 bound to DPC micelles adopts a α-helical secondary structure involving residues 4-19. The C-terminal residues converge to a lose β-turn structure. The results of this investigation indicate hydrophobic interactions are the major contributors to stabilizing the induced helical structure of the micelle-bound peptides. Electrostatic interactions between the polar head groups of the micelle and the cationic side chains of the peptides define the positions along the peptide backbone where the helical structures begin and end.

Original languageEnglish (US)
Pages (from-to)459-470
Number of pages12
JournalBiopolymers
Volume68
Issue number4
DOIs
StatePublished - Apr 1 2003

Fingerprint

Magainins
Surface Properties
Sodium dodecyl sulfate
Micelles
Static Electricity
Sodium Dodecyl Sulfate
Peptides
Surface properties
Conformations
Electrostatics
Amides
Molecular modeling
Coulomb interactions
Hydrophobic and Hydrophilic Interactions
dodecylphosphocholine
Nuclear magnetic resonance

Keywords

  • Antimicrobial peptides
  • Magainins
  • Molecular modeling
  • NMR

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles. / Hicks, Rickey Paige; Mones, Erin; Kim, Hanah; Koser, Brandon W.; Nichols, Daniel A.; Bhattacharjee, Apurba K.

In: Biopolymers, Vol. 68, No. 4, 01.04.2003, p. 459-470.

Research output: Contribution to journalArticle

Hicks, Rickey Paige ; Mones, Erin ; Kim, Hanah ; Koser, Brandon W. ; Nichols, Daniel A. ; Bhattacharjee, Apurba K. / Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles. In: Biopolymers. 2003 ; Vol. 68, No. 4. pp. 459-470.
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