Pfg-nmr investigations of the binding of cationic neuropeptides to anionic and zwitterionic micelles

Tracy L. Whitehead, Lucretia M. Jones, Rickey Paige Hicks

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The mechanism by which peptides bind to micelles is believed to be a two-phase process, involving (i) initial electrostatic interactions between the peptide and micelle surface, followed by (ii) hydrophobic interactions between peptide side chains and the micelle core. To better characterize the electrostatic portion of this process, a series of pulse field gradient nuclear magnetic resonance (PFG-NMR) spectroscopic experiments were conducted on a group of neuropeptides with varying net cationic charges (+1 to +3) and charge location to determine both their diffusion coefficients and partition coefficients when in the presence of detergent micelles. Two types of micelles were chosen for the study, namely anionic sodium dodecylsulfate (SDS) and zwitterionic dodecylphosphocholine (DPC) micelles. Results obtained from this investigation indicate that in the case of the anionic SDS micelles, peptides with a larger net positive charge bind to a greater extent than those with a lesser net positive charge (bradykinin > substance P > neurokinin A > Met-enkephalin). In contrast, when in the presence of zwitterionic DPC micelles, the degree of mixed-charge nature of the peptide affects binding (neurokinin A > substance P > Met-enkephalin > bradykinin). Partition coefficients between the peptides and the micelles follow similar trends for both micelle types. Diffusion coefficients for the peptides in SDS micelles, when ranked from largest to smallest, follow a trend where increasing net positive charge results in the smallest diffusion coefficient: Met-enkephalin > neurokinin A > bradykinin > substance P. Diffusion coefficients when in the presence of DPC micelles, when ranked from largest to smallest, follow a trend where the presence of negatively-charged side chains results in the smallest diffusion coefficient: bradykinin > Met-enkephalin > substance P > neurokinin A.

Original languageEnglish (US)
Pages (from-to)567-576
Number of pages10
JournalJournal of Biomolecular Structure and Dynamics
Volume21
Issue number4
DOIs
StatePublished - Jan 1 2004

Fingerprint

Micelles
Neuropeptides
Neurokinin A
Methionine Enkephalin
Peptides
Bradykinin
Substance P
Sodium
Static Electricity
Hydrophobic and Hydrophilic Interactions
Detergents
Magnetic Resonance Spectroscopy

Keywords

  • Dodecylphosphocholine (DPC)
  • Micelles
  • Neuropeptides
  • Pulse Field Gradient Nuclear Magnetic Resonance (PFG-NMR) spectroscopy
  • Sodium Dodecylsulfate (SDS)
  • Substance P
  • Tachykinins

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Pfg-nmr investigations of the binding of cationic neuropeptides to anionic and zwitterionic micelles. / Whitehead, Tracy L.; Jones, Lucretia M.; Hicks, Rickey Paige.

In: Journal of Biomolecular Structure and Dynamics, Vol. 21, No. 4, 01.01.2004, p. 567-576.

Research output: Contribution to journalArticle

Whitehead, Tracy L. ; Jones, Lucretia M. ; Hicks, Rickey Paige. / Pfg-nmr investigations of the binding of cationic neuropeptides to anionic and zwitterionic micelles. In: Journal of Biomolecular Structure and Dynamics. 2004 ; Vol. 21, No. 4. pp. 567-576.
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AB - The mechanism by which peptides bind to micelles is believed to be a two-phase process, involving (i) initial electrostatic interactions between the peptide and micelle surface, followed by (ii) hydrophobic interactions between peptide side chains and the micelle core. To better characterize the electrostatic portion of this process, a series of pulse field gradient nuclear magnetic resonance (PFG-NMR) spectroscopic experiments were conducted on a group of neuropeptides with varying net cationic charges (+1 to +3) and charge location to determine both their diffusion coefficients and partition coefficients when in the presence of detergent micelles. Two types of micelles were chosen for the study, namely anionic sodium dodecylsulfate (SDS) and zwitterionic dodecylphosphocholine (DPC) micelles. Results obtained from this investigation indicate that in the case of the anionic SDS micelles, peptides with a larger net positive charge bind to a greater extent than those with a lesser net positive charge (bradykinin > substance P > neurokinin A > Met-enkephalin). In contrast, when in the presence of zwitterionic DPC micelles, the degree of mixed-charge nature of the peptide affects binding (neurokinin A > substance P > Met-enkephalin > bradykinin). Partition coefficients between the peptides and the micelles follow similar trends for both micelle types. Diffusion coefficients for the peptides in SDS micelles, when ranked from largest to smallest, follow a trend where increasing net positive charge results in the smallest diffusion coefficient: Met-enkephalin > neurokinin A > bradykinin > substance P. Diffusion coefficients when in the presence of DPC micelles, when ranked from largest to smallest, follow a trend where the presence of negatively-charged side chains results in the smallest diffusion coefficient: bradykinin > Met-enkephalin > substance P > neurokinin A.

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