Recently, we reported the bioisosteric substitution of a guanidine by an acylguanidine entity in argininamide-type neuropeptide Y (NPY) Y 1 receptor (Y 1 R) antagonists, such as BIBP 3226 [1] (1; Scheme 1), to be an effective strategy for the [a] Dr.
[3H]pBC 264, first highly potent and very selective radioligand for CCK-B receptors
β Scribed by Christiane Durieux; Pierre-Jean Corringer; Florence Bergeron; Bernard P. Roques
- Book ID
- 115882602
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- English
- Weight
- 181 KB
- Volume
- 168
- Category
- Article
- ISSN
- 0014-2999
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## Abstract Among the CCKβB receptor agonists reported to date, the two modified peptides BC 264 and BC 254 display a high affinity and selectivity for this binding site and are highly protected from enzymatic degradation. Recently, we reported the biological properties of a tritiated analog of thi
The new CCKB analog, Boc-Tyr (S0,H)-gNle-mGly-Trp-(NMe)-Nle-Asp-PheNHJBC 264) exhibited a high affinity (KI = 0.39 2 0.15 nM) and selectivity for central (B) versus peripheral (A) receptors (KI CCKAKI CCKB = 910) in the rat. In agreement with these binding studies, BC 264 was a t least 50 times more