Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin

Krzysztof Darłak; Zbigniew Grzonka; Pawel Krzaścik; Piotr Janicki; S. Witold Gumułka

doi:10.1016/0196-9781(84)90007-X

Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin

Krzysztof Darłak, Zbigniew Grzonka, Pawel Krzaścik, Piotr Janicki, S. Witold Gumułka

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Abstract

Seventeen analogues of dermorphin were synthesized and bio-assayed to determine the influence of side chains of the individual amino acid residues forming the sequence of dermorphin on the biological activity of this opioid peptide. Syntheses were carried out using solid-phase procedure, and the analogues obtained were purified by gel filtration on Sephadex G-10. Biological activities determined in guinea pig ileum (GPI) and mouse vas deferens (MVD) tests showed that the N-terminal tetrapeptide is responsible for the activity of dermorphin. Substitutions in the C-terminal fragment, particularly in position 5, for other amino acid residues results in substantial differentiation towards μ and δ receptors.

Original language	English (US)
Pages (from-to)	687-689
Number of pages	3
Journal	Peptides
Volume	5
Issue number	4
DOIs	https://doi.org/10.1016/0196-9781(84)90007-X
State	Published - 1984

All Science Journal Classification (ASJC) codes

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

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10.1016/0196-9781(84)90007-X

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title = "Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin",

abstract = "Seventeen analogues of dermorphin were synthesized and bio-assayed to determine the influence of side chains of the individual amino acid residues forming the sequence of dermorphin on the biological activity of this opioid peptide. Syntheses were carried out using solid-phase procedure, and the analogues obtained were purified by gel filtration on Sephadex G-10. Biological activities determined in guinea pig ileum (GPI) and mouse vas deferens (MVD) tests showed that the N-terminal tetrapeptide is responsible for the activity of dermorphin. Substitutions in the C-terminal fragment, particularly in position 5, for other amino acid residues results in substantial differentiation towards μ and δ receptors.",

author = "Krzysztof Dar{\l}ak and Zbigniew Grzonka and Pawel Krza{\'s}cik and Piotr Janicki and Gumu{\l}ka, {S. Witold}",

note = "Funding Information: This work was supported in part by the Polish Academy of Sciences Grant MR.I. 12.1.6.3.",

year = "1984",

doi = "10.1016/0196-9781(84)90007-X",

language = "English (US)",

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pages = "687--689",

journal = "Peptides",

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T1 - Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin

AU - Darłak, Krzysztof

AU - Grzonka, Zbigniew

AU - Krzaścik, Pawel

AU - Janicki, Piotr

AU - Gumułka, S. Witold

N1 - Funding Information: This work was supported in part by the Polish Academy of Sciences Grant MR.I. 12.1.6.3.

PY - 1984

Y1 - 1984

N2 - Seventeen analogues of dermorphin were synthesized and bio-assayed to determine the influence of side chains of the individual amino acid residues forming the sequence of dermorphin on the biological activity of this opioid peptide. Syntheses were carried out using solid-phase procedure, and the analogues obtained were purified by gel filtration on Sephadex G-10. Biological activities determined in guinea pig ileum (GPI) and mouse vas deferens (MVD) tests showed that the N-terminal tetrapeptide is responsible for the activity of dermorphin. Substitutions in the C-terminal fragment, particularly in position 5, for other amino acid residues results in substantial differentiation towards μ and δ receptors.

AB - Seventeen analogues of dermorphin were synthesized and bio-assayed to determine the influence of side chains of the individual amino acid residues forming the sequence of dermorphin on the biological activity of this opioid peptide. Syntheses were carried out using solid-phase procedure, and the analogues obtained were purified by gel filtration on Sephadex G-10. Biological activities determined in guinea pig ileum (GPI) and mouse vas deferens (MVD) tests showed that the N-terminal tetrapeptide is responsible for the activity of dermorphin. Substitutions in the C-terminal fragment, particularly in position 5, for other amino acid residues results in substantial differentiation towards μ and δ receptors.

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Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin

Abstract

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