Biological properties of Phe°-opioid peptide analogues

Andrzej W. Lipkowski; Aleksandra Misicka; Keiko Hosohata; Peg Davis; Henry I. Yamamura; Frank Porreca; Victor J. Hruby

doi:10.1016/S0024-3205(00)00993-0

Biological properties of Phe°-opioid peptide analogues

Andrzej W. Lipkowski, Aleksandra Misicka, Keiko Hosohata, Peg Davis, Henry I. Yamamura, Frank Porreca, Victor J. Hruby

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Biological properties of new analogues, which represent Phe°-propeptides of a variety of opioid peptides, are described. All Phe°-opioid analogues expressed both receptor binding affinities and in vitro biological activities at least at the level of the primary opioid peptides. Surprisingly, some of the propeptides expressed slightly higher activity than the primary opioid peptides. Nevertheless, no significant shift in receptor selectivity was observed, which indicate that these Phe°-analogues undoubtedly are propeptides. The possible role of membrane proteolytic enzymes associated with opioid receptors in transformation of propeptides is discussed.

Original language	English (US)
Pages (from-to)	969-972
Number of pages	4
Journal	Life Sciences
Volume	68
Issue number	8
DOIs	https://doi.org/10.1016/S0024-3205(00)00993-0
State	Published - Jan 12 2001

Keywords

Drug design
Opioid peptides
Prodrugs

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Pharmacology, Toxicology and Pharmaceutics(all)

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10.1016/S0024-3205(00)00993-0

Cite this

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title = "Biological properties of Phe°-opioid peptide analogues",

abstract = "Biological properties of new analogues, which represent Phe°-propeptides of a variety of opioid peptides, are described. All Phe°-opioid analogues expressed both receptor binding affinities and in vitro biological activities at least at the level of the primary opioid peptides. Surprisingly, some of the propeptides expressed slightly higher activity than the primary opioid peptides. Nevertheless, no significant shift in receptor selectivity was observed, which indicate that these Phe°-analogues undoubtedly are propeptides. The possible role of membrane proteolytic enzymes associated with opioid receptors in transformation of propeptides is discussed.",

keywords = "Drug design, Opioid peptides, Prodrugs",

author = "Lipkowski, {Andrzej W.} and Aleksandra Misicka and Keiko Hosohata and Peg Davis and Yamamura, {Henry I.} and Frank Porreca and Hruby, {Victor J.}",

note = "Funding Information: We thank The National Institute of Drug Abuse, U.S. Public Health Service Grant DA 06284 and the Medical Research Centre of Polish Academy of Sciences for supporting this work. The views expressed here are those of the authors and do not necessarily reflect those of the USPHS.",

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T1 - Biological properties of Phe°-opioid peptide analogues

AU - Lipkowski, Andrzej W.

AU - Misicka, Aleksandra

AU - Hosohata, Keiko

AU - Davis, Peg

AU - Yamamura, Henry I.

AU - Porreca, Frank

AU - Hruby, Victor J.

N1 - Funding Information: We thank The National Institute of Drug Abuse, U.S. Public Health Service Grant DA 06284 and the Medical Research Centre of Polish Academy of Sciences for supporting this work. The views expressed here are those of the authors and do not necessarily reflect those of the USPHS.

PY - 2001/1/12

Y1 - 2001/1/12

N2 - Biological properties of new analogues, which represent Phe°-propeptides of a variety of opioid peptides, are described. All Phe°-opioid analogues expressed both receptor binding affinities and in vitro biological activities at least at the level of the primary opioid peptides. Surprisingly, some of the propeptides expressed slightly higher activity than the primary opioid peptides. Nevertheless, no significant shift in receptor selectivity was observed, which indicate that these Phe°-analogues undoubtedly are propeptides. The possible role of membrane proteolytic enzymes associated with opioid receptors in transformation of propeptides is discussed.

AB - Biological properties of new analogues, which represent Phe°-propeptides of a variety of opioid peptides, are described. All Phe°-opioid analogues expressed both receptor binding affinities and in vitro biological activities at least at the level of the primary opioid peptides. Surprisingly, some of the propeptides expressed slightly higher activity than the primary opioid peptides. Nevertheless, no significant shift in receptor selectivity was observed, which indicate that these Phe°-analogues undoubtedly are propeptides. The possible role of membrane proteolytic enzymes associated with opioid receptors in transformation of propeptides is discussed.

KW - Drug design

KW - Opioid peptides

KW - Prodrugs

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Biological properties of Phe°-opioid peptide analogues

Abstract

Keywords

ASJC Scopus subject areas

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