scholarly journals Thermodynamics of the binding of Substance P to lipid membranes

2017 ◽  
Vol 30 (2) ◽  
pp. 89-95
Author(s):  
Woong Hyoung Lee ◽  
Chul Kim
Keyword(s):  
Substance P ◽  
Lipid Membranes

scholarly journals Conformation and self-association of the peptide hormone substance P: Fourier-transform infrared spectroscopic study

1994 ◽  
Vol 301 (3) ◽  
pp. 667-670 ◽  
Author(s):  
L P Choo ◽  
M Jackson ◽  
H H Mantsch
Keyword(s):  
Aqueous Solution ◽  
Fourier Transform ◽  
Secondary Structure ◽  
Substance P ◽  
Lipid Membranes ◽  
Membrane Surface ◽  
Peptide Hormone ◽  
Infrared Spectroscopic Study ◽  
Active Conformation ◽  
Self Association

Fourier-transform i.r. (f.t.i.r.) spectroscopy has been applied to the study of the conformational properties of substance P in aqueous solution. Spectra were obtained in the presence of lipid membranes and Ca2+ to assess the role of these factors in induction of the active conformation of the peptide. In aqueous solution substance P was found to be predominantly unstructured at physiological p2H, where the lack of long-range order is probably related to charge repulsion along the peptide chain. However, substance P aggregated in aqueous solution at p2H > 10.0. Little or no induction of secondary structure was seen on addition of the peptide to negatively charged bilayers, suggesting that interaction with a membrane surface does not play an important role in the stabilization of the active conformation of the peptide. In fact, substance P was found to aggregate in the presence of charged lipids, which would tend to hinder rather than enhance interaction with the receptor. We propose a model for the aggregation of substance P at the bilayer surface, based on our studies of the effect of p2H and lipid/peptide ratio on spectra. Addition of Ca2+ had no effect upon the secondary structure of the peptide or on its interactions with membranes.

Reversible binding of substance P to artificial lipid membranes studied by capacitance minimization techniques

1989 ◽  
Vol 34 (2) ◽  
pp. 103-114 ◽  
Author(s):  
D.F. Sargent ◽  
J.W. Bean ◽  
R. Schwyzer
Keyword(s):  
Substance P ◽  
Lipid Membranes ◽  
Reversible Binding

Binding of Substance P Agonists to Lipid Membranes and to the Neurokinin-1 Receptor†

Biochemistry ◽  
1996 ◽  
Vol 35 (14) ◽  
pp. 4365-4374 ◽  
Author(s):  
Anna Seelig ◽  
Thomas Alt ◽  
Sandra Lotz ◽  
Günter Hölzemann
Keyword(s):  
Substance P ◽  
Lipid Membranes ◽  
Neurokinin 1 Receptor ◽  
Neurokinin 1

Redox Reactions in Lipid Membranes as a Model for Primordial Energy-Conserving Systems

1997 ◽  
Vol 161 ◽  
pp. 437-442
Author(s):  
Salvatore Di Bernardo ◽  
Romana Fato ◽  
Giorgio Lenaz
Keyword(s):  
Experimental Evidence ◽  
Lipid Membranes ◽  
Energy Supply ◽  
Redox Reactions ◽  
Living Systems ◽  
Asymmetric Distribution ◽  
Conservation Of Energy ◽  
Asymmetrical Distribution ◽  
Energy Conserving ◽  
Living Organisms

AbstractOne of the peculiar aspects of living systems is the production and conservation of energy. This aspect is provided by specialized organelles, such as the mitochondria and chloroplasts, in developed living organisms. In primordial systems lacking specialized enzymatic complexes the energy supply was probably bound to the generation and maintenance of an asymmetric distribution of charged molecules in compartmentalized systems. On the basis of experimental evidence, we suggest that lipophilic quinones were involved in the generation of this asymmetrical distribution of charges through vectorial redox reactions across lipid membranes.

Observation of Concanavalin-A receptors on hydrated planar erythrocyte membrane film by in situ electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 608-609
Author(s):  
Neng-Bo He ◽  
S.W. Hui
Keyword(s):  
Lipid Bilayers ◽  
Erythrocyte Membrane ◽  
Lipid Membranes ◽  
Surface Film ◽  
Biological Membranes ◽  
Electron Microscopic Observation ◽  
Electron Microscopic ◽  
Black Lipid Membranes ◽  
Fine Mesh ◽  
Planar Films

Monolayers and planar "black" lipid membranes have been widely used as models for studying the structure and properties of biological membranes. Because of the lack of a suitable method to prepare these membranes for electron microscopic observation, their ultrastructure is so far not well understood. A method of forming molecular bilayers over the holes of fine mesh grids was developed by Hui et al. to study hydrated and unsupported lipid bilayers by electron diffraction, and to image phase separated domains by diffraction contrast. We now adapted the method of Pattus et al. of spreading biological membranes vesicles on the air-water interfaces to reconstitute biological membranes into unsupported planar films for electron microscopic study. hemoglobin-free human erythrocyte membrane stroma was prepared by hemolysis. The membranes were spreaded at 20°C on balanced salt solution in a Langmuir trough until a surface pressure of 20 dyne/cm was reached. The surface film was repeatedly washed by passing to adjacent troughs over shallow partitions (fig. 1).

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