Abstract
NMR and CD studies have been used to analyze the model membrane-bound structure of the neuropeptide substance P (RPKPQQFFGLM-NH2, SP), which has previously been proposed as the NK1 receptor active form. Conformations were determined for the SP in the presence of aqueous solutions of zwitterionic dodecylphosphocholine (DPC) and anionic sodium dodecylsulfate (SDS) micelles. The two structures are similar, although fast exchange between free and bound forms was observed for SP with DPC micelles, and predominantly bound characteristics were found for SP in SDS. The addition of 150-200 mM NaCl had no observable effect on the bound conformation in either case. Thus, the structure of SP at a micelle surface is determined largely by hydrophobic forces, and the electrostatic interactions determine the amount of SP that is bound.
MeSH Terms
Amino Acid Sequence
Biophysical Phenomena
Biophysics
Circular Dichroism
Electrochemistry
Hydrogen-Ion Concentration
Lipids/chemistry
Magnetic Resonance Spectroscopy
Micelles
Models, Molecular
Molecular Sequence Data
Phosphorylcholine/analogs & derivatives,chemistry
Protein Conformation
Sodium Dodecyl Sulfate
Solutions
Substance P/chemistry,genetics
Chemicals
Lipids
Micelles
Solutions
Phosphorylcholine
Substance P
Sodium Dodecyl Sulfate
dodecylphosphocholine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Keire D A
Beckman Research Institute of the City of Hope, California 91010-0269, USA. dak@ernst.coh.org
Fletcher T G
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