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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Keire DA,Fletcher TGdoi
10.1016/S0006-3495(96)79734-5subject
Has Abstractpub_date
1996-04-01 00:00:00pages
1716-27issue
4eissn
0006-3495issn
1542-0086pii
S0006-3495(96)79734-5journal_volume
70pub_type
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