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PMID: 8785330 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The conformation of substance P in lipid environments.

Biophysical journal ·Vol. 70 ·No. 4 ·1996-04-00 ·Pages 1716-27

Keire DA, Fletcher TG

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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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1996-04-00
Pages
1716-27
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1225140
Subset
IM
Grants
NCI NIH HHS · CA33572 · United States
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