Preferential conformation of substance P in solution
- 1 January 1986
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 154 (1) , 77-85
- https://doi.org/10.1111/j.1432-1033.1986.tb09361.x
Abstract
The three-dimensional structure of substance P has been studied by 1H-NMR, (500 MHz), and by circular dichroism (CD) in different solvents. The analysis of the different NMR parameters suggest that substance P adopts a rather extended structure in dimethylsulfoxide and pyridine. In water, besides the aggregation phenomenon, the monomeric substance P presents a complex conformational equilibrium. The addition of sodium dodecylsulfate to the aqueous solution induces, as shown by CD spectroscopy, a preferential .alpha.-helical conformation. And in methanol three structural conclusions may be drawn: the flexibility of the N-terminal Arg-Pro-Lys, the .alpha.-helical structure of Pro4-Gln5-Gln6-Phe7-Phe8 and the interaction of the C-terminal carboxamide with the primary amides from both glutamines.This publication has 40 references indexed in Scilit:
- Self‐association of the neuroregulatory peptide substance P and its C‐terminal sequencesBiopolymers, 1984
- Interactions of Lipid Bilayers with Corticotropin, Dynorphin, and Enkephalin PeptidesPublished by Walter de Gruyter GmbH ,1983
- Properties of a 125I-substance P derivative binding to synaptosomes from various brain structures and the spinal cord of the ratNaunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie, 1983
- 1H‐NMR studies on substance P hexapeptide analogsBiopolymers, 1983
- Conformation and Biological Activity of Cyclic PeptidesAngewandte Chemie International Edition in English, 1982
- Modifications of drinking behaviour and of arterial blood pressure induced by tachykinins in rats and pigeonsPsychopharmacology, 1980
- Substance P: Model studies of its binding to phospholipidsNaunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie, 1979
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979
- NMR observation of gramicidin A′ in phosphatidylcholine vesiclesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977
- Interaction of glucagon with dimyristoyl glycerophosphocholineBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977