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Radioligand binding properties of VV-hemorphin 7, an atypical opioid peptide.

Abstract：

:Receptor binding properties of the hemoglobin-derived nonapeptide VV-hemorphin 7 (Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe-OH) were studied using both the unlabelled form and tritium-labelled derivative of the peptide. In binding studies using selective opioid radioligands, VV-hemorphin 7 exhibited a rank order of potency of mu > kappa > delta. VV-hemorphin 7 was tritiated resulting in a compound with 1.03 TBq/mmol (27.8 Ci/mmol) specific radioactivity. The maximal number of binding sites was found to be 66.5 pmol/mg protein with an affinity of 82.1 nM in rat brain membranes. In competition studies, marked similarity was observed to the binding profile of the naturally occurring opioid heptapeptide Met-enkephalin-Arg-Phe (MERF) and its analogues to their naloxone-insensitive binding site. The common -Arg-Phe sequence at the carboxyl terminal end, which is similar to those of other endogenous peptides (-Arg-Phe-NH(2) in neuropeptide FF and FMRF-NH(2)) brings attention to the C-terminal end of the molecule and points to the possible existence of a common nonopioid binding site in mammals.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Szikra J,Benyhe S,Orosz G,Darula Z,Piot JM,Fruitier I,Monory K,Hanoune J,Borsodi A

doi

10.1006/bbrc.2001.4397

subject

Has Abstract

pub_date

2001-03-02 00:00:00

pages

670-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)94397-9

journal_volume

281

pub_type

杂志文章

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