Fluorescence studies of endothelin-1.

Abstract:

:Fluorescence measurements and singlet singlet energy transfer experiments on endothelin-1 provide information on the conformation of this peptide in dilute aqueous solution. The tyrosine fluorescence quantum yield in the absence of transfer (in [Phe(21)]endothelin-1) is relatively large (?(tyr) = 0.39), indicating the side-chain is oriented away from fluorescence quenching groups such as the two disulfide bonds of the peptide. The fluorescence emission maximum (? = 351 nm) and quantum yield (?(trp) = 0.099) of tryptophan in endothelin-I suggests that this residue is fully accessible to the solvent and that the indole ring is not located near the fluorescence quenching histidinium moiety or the disulfide bonds. Singlet-singlet fluorescence energy transfer measurements of the Tyr(13)/Trp(21) intramolecular distance by both donor fluorescence quenching and relative enhancement of acceptor fluorescence yield a distance of about 12.8 +/- 0.6 A ? . Molecular modeling of a fully extended C-terminal hexapeptide indicates a Tyr(13)/Trp(21) distance of about 25 A. Thus, the C-terminal residues must bend back towards the bicyclic portion of the molecule.

journal_name

Neurochem Int

authors

Pelton JT

doi

10.1016/0197-0186(91)90144-3

subject

Has Abstract

pub_date

1991-01-01 00:00:00

pages

485-9

issue

4

eissn

0197-0186

issn

1872-9754

pii

0197-0186(91)90144-3

journal_volume

18

pub_type

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