In vitro stability of some reduced peptide bond pseudopeptide analogues of dynorphin A

Jean Philippe Meyer; Terrence J. Gillespie; Sharon Hom; Victor J. Hruby; Thomas P. Davis

doi:10.1016/0196-9781(95)02005-H

In vitro stability of some reduced peptide bond pseudopeptide analogues of dynorphin A

Jean Philippe Meyer, Terrence J. Gillespie, Sharon Hom, Victor J. Hruby, Thomas P. Davis

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

19 Scopus citations

Abstract

Eight analogues of DYN A(1-11)-NH₂ incorporating the nonhydrolyzable Ψ[CH₂-NH] peptide bond surrogate were tested for their in vitro enzymatic stability in mouse brain homogenates. Results show that the Leu⁵-Arg⁶ and to a lesser extent the Arg⁷-Ile⁸ and Ile⁸-Arg⁹ peptide bonds are the more susceptible to enzymatic cleavage in the native peptide. (Leu⁵Ψ[CH₂-NH]Arg⁶)DYN A(1-11)-NH₂ exhibits an almost complete resistance to enzymatic cleavage with a half-life greater than 500 min in brain, compared to 42 min for the standard peptide, DYN A(1-11)-NH₂.

Original language	English (US)
Pages (from-to)	1215-1219
Number of pages	5
Journal	Peptides
Volume	16
Issue number	7
DOIs	https://doi.org/10.1016/0196-9781(95)02005-H
State	Published - 1995

Keywords

Dynorphin A
Enzymatic stability
Enzymes
Ψ[CH-NH] reduced bond

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

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10.1016/0196-9781(95)02005-H

Cite this

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title = "In vitro stability of some reduced peptide bond pseudopeptide analogues of dynorphin A",

abstract = "Eight analogues of DYN A(1-11)-NH2 incorporating the nonhydrolyzable Ψ[CH2-NH] peptide bond surrogate were tested for their in vitro enzymatic stability in mouse brain homogenates. Results show that the Leu5-Arg6 and to a lesser extent the Arg7-Ile8 and Ile8-Arg9 peptide bonds are the more susceptible to enzymatic cleavage in the native peptide. (Leu5Ψ[CH2-NH]Arg6)DYN A(1-11)-NH2 exhibits an almost complete resistance to enzymatic cleavage with a half-life greater than 500 min in brain, compared to 42 min for the standard peptide, DYN A(1-11)-NH2.",

keywords = "Dynorphin A, Enzymatic stability, Enzymes, Ψ[CH-NH] reduced bond",

author = "Meyer, {Jean Philippe} and Gillespie, {Terrence J.} and Sharon Hom and Hruby, {Victor J.} and Davis, {Thomas P.}",

year = "1995",

doi = "10.1016/0196-9781(95)02005-H",

language = "English (US)",

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pages = "1215--1219",

journal = "Peptides",

issn = "0196-9781",

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TY - JOUR

T1 - In vitro stability of some reduced peptide bond pseudopeptide analogues of dynorphin A

AU - Meyer, Jean Philippe

AU - Gillespie, Terrence J.

AU - Hom, Sharon

AU - Hruby, Victor J.

AU - Davis, Thomas P.

PY - 1995

Y1 - 1995

N2 - Eight analogues of DYN A(1-11)-NH2 incorporating the nonhydrolyzable Ψ[CH2-NH] peptide bond surrogate were tested for their in vitro enzymatic stability in mouse brain homogenates. Results show that the Leu5-Arg6 and to a lesser extent the Arg7-Ile8 and Ile8-Arg9 peptide bonds are the more susceptible to enzymatic cleavage in the native peptide. (Leu5Ψ[CH2-NH]Arg6)DYN A(1-11)-NH2 exhibits an almost complete resistance to enzymatic cleavage with a half-life greater than 500 min in brain, compared to 42 min for the standard peptide, DYN A(1-11)-NH2.

AB - Eight analogues of DYN A(1-11)-NH2 incorporating the nonhydrolyzable Ψ[CH2-NH] peptide bond surrogate were tested for their in vitro enzymatic stability in mouse brain homogenates. Results show that the Leu5-Arg6 and to a lesser extent the Arg7-Ile8 and Ile8-Arg9 peptide bonds are the more susceptible to enzymatic cleavage in the native peptide. (Leu5Ψ[CH2-NH]Arg6)DYN A(1-11)-NH2 exhibits an almost complete resistance to enzymatic cleavage with a half-life greater than 500 min in brain, compared to 42 min for the standard peptide, DYN A(1-11)-NH2.

KW - Dynorphin A

KW - Enzymatic stability

KW - Enzymes

KW - Ψ[CH-NH] reduced bond

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DO - 10.1016/0196-9781(95)02005-H

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AN - SCOPUS:0028808566

SN - 0196-9781

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EP - 1219

JO - Peptides

JF - Peptides

IS - 7

ER -

In vitro stability of some reduced peptide bond pseudopeptide analogues of dynorphin A

Abstract

Keywords

ASJC Scopus subject areas

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