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Howl J, New DC, Wheatley M. Design and synthesis of heterofunctional V1a-selective vasopressin receptor ligands with lysine at position 9. J Mol Endocrinol. 1992;9(2):123-9doi: 10.1677/jme.0.0090123.
Howl, J., New, D. C., & Wheatley, M. (1992). Design and synthesis of heterofunctional V1a-selective vasopressin receptor ligands with lysine at position 9. Journal of molecular endocrinology, 9(2), 123-9. https://doi.org/10.1677/jme.0.0090123
Howl, J, et al. "Design and synthesis of heterofunctional V1a-selective vasopressin receptor ligands with lysine at position 9." Journal of molecular endocrinology vol. 9,2 (1992): 123-9. doi: https://doi.org/10.1677/jme.0.0090123
Howl J, New DC, Wheatley M. Design and synthesis of heterofunctional V1a-selective vasopressin receptor ligands with lysine at position 9. J Mol Endocrinol. 1992 Oct;9(2):123-9. doi: 10.1677/jme.0.0090123. PMID: 1418383.
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J Mol Endocrinol. 1992 Oct;9(2):123-9. doi: 10.1677/jme.0.0090123.

Design and synthesis of heterofunctional V1a-selective vasopressin receptor ligands with lysine at position 9.

Journal of molecular endocrinology

J Howl, D C New, M Wheatley

Affiliations

  1. School of Biochemistry, University of Birmingham, Edgbaston, U.K.

PMID: 1418383 DOI: 10.1677/jme.0.0090123

Abstract

A peptide analogue of [8-arginine]vasopressin (AVP) with Lys substituted for Gly at position 9 ([d(CH2)5Tyr(Me)2LysNH2(9)]AVP; ALVP) has been synthesized as a precursor for the production of heterofunctional vasopressin receptor ligands. Three heterofunctional ligands have been prepared by attaching biotin and a photoreactive cross-linker capable of iodination, either alone or in combination, to the epsilon-amino group of Lys at position 9 in ALVP. The binding characteristics of these novel ligands have been determined at the V1a and V2 vasopressin receptors by employing membrane preparations of rat liver and kidney respectively. All of the analogues synthesized during the course of this study bound selectively, and with high affinity, to the V1a vasopressin receptor subtype. Our results demonstrate that the strategies described in this paper provide a convenient means of synthesizing heterofunctional vasopressin receptor ligands with preservation of subtype-specific, high affinity binding characteristics. These parameters establish the potential value of the analogues as probes for investigating V1a receptor structure and function.

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