Adsorption of aminopyridines to phosphatidylserine vesicles

Intrinsic association constants were determined for a series of aminopyridines on phosphatidylserine vesicles, through determination of electrophoretic mobility. The magnitudes of the constants were such that depolarization of the nerve terminal through binding to negative phospholipids seems unlike...

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Bibliographic Details
Main Author: Wright, Colin
Format: Others
Published: PDXScholar 1986
Subjects:
Online Access:https://pdxscholar.library.pdx.edu/open_access_etds/3686
https://pdxscholar.library.pdx.edu/cgi/viewcontent.cgi?article=4695&context=open_access_etds
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spelling ndltd-pdx.edu-oai-pdxscholar.library.pdx.edu-open_access_etds-46952019-10-20T04:31:36Z Adsorption of aminopyridines to phosphatidylserine vesicles Wright, Colin Intrinsic association constants were determined for a series of aminopyridines on phosphatidylserine vesicles, through determination of electrophoretic mobility. The magnitudes of the constants were such that depolarization of the nerve terminal through binding to negative phospholipids seems unlikely to occur. The aminopyridines all had association constants between one half and one sixtieth the association constant of calcium. The aminopyridines probably block potassium channels in their enhancement of synaptic transmission. An interesting correlation was noted in that the ranking of the aminopyridines in terms of their affinity for these lipids was approximately the same as the ranking of their enhancement of synaptic transmission in a wide variety of biological preparations. A possible mechanism for this correlation is that adsorption of these drugs 2 to lipid membranes is the initial and rate-limiting step in their action. 1986-01-01T08:00:00Z text application/pdf https://pdxscholar.library.pdx.edu/open_access_etds/3686 https://pdxscholar.library.pdx.edu/cgi/viewcontent.cgi?article=4695&context=open_access_etds Dissertations and Theses PDXScholar Adsorption (Biology) Aminopyridines Phosphatidylserine Neural transmission Biology
collection NDLTD
format Others
sources NDLTD
topic Adsorption (Biology)
Aminopyridines
Phosphatidylserine
Neural transmission
Biology
spellingShingle Adsorption (Biology)
Aminopyridines
Phosphatidylserine
Neural transmission
Biology
Wright, Colin
Adsorption of aminopyridines to phosphatidylserine vesicles
description Intrinsic association constants were determined for a series of aminopyridines on phosphatidylserine vesicles, through determination of electrophoretic mobility. The magnitudes of the constants were such that depolarization of the nerve terminal through binding to negative phospholipids seems unlikely to occur. The aminopyridines all had association constants between one half and one sixtieth the association constant of calcium. The aminopyridines probably block potassium channels in their enhancement of synaptic transmission. An interesting correlation was noted in that the ranking of the aminopyridines in terms of their affinity for these lipids was approximately the same as the ranking of their enhancement of synaptic transmission in a wide variety of biological preparations. A possible mechanism for this correlation is that adsorption of these drugs 2 to lipid membranes is the initial and rate-limiting step in their action.
author Wright, Colin
author_facet Wright, Colin
author_sort Wright, Colin
title Adsorption of aminopyridines to phosphatidylserine vesicles
title_short Adsorption of aminopyridines to phosphatidylserine vesicles
title_full Adsorption of aminopyridines to phosphatidylserine vesicles
title_fullStr Adsorption of aminopyridines to phosphatidylserine vesicles
title_full_unstemmed Adsorption of aminopyridines to phosphatidylserine vesicles
title_sort adsorption of aminopyridines to phosphatidylserine vesicles
publisher PDXScholar
publishDate 1986
url https://pdxscholar.library.pdx.edu/open_access_etds/3686
https://pdxscholar.library.pdx.edu/cgi/viewcontent.cgi?article=4695&context=open_access_etds
work_keys_str_mv AT wrightcolin adsorptionofaminopyridinestophosphatidylserinevesicles
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