New features of the δ opioid receptor: Conformational properties of deltorphin I analogues
Deltorphin I is an opioid peptide of sequence H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH 2, recently isolated from the skin of Phyllomedusa bicolor. Its enormous selectivity towards the δ opioid receptor and the similarity of the conformation of the N-terminal part of the sequence with that of dermorphin (H...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1990-06, Vol.169 (2), p.617-622 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Balboni, G. Marastoni, M. Picone, D. Salvadori, S. Tancredi, T. Temussi, P.A. Tomatis, R. |
| description | Deltorphin I is an opioid peptide of sequence H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH
2, recently isolated from the skin of
Phyllomedusa bicolor. Its enormous selectivity towards the δ opioid receptor and the similarity of the conformation of the N-terminal part of the sequence with that of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH
2), a μ selective peptide, prompted the synthesis, biological evaluation and comparative conformational study of four analogs. A
1H-NMR study showed that the conformational preferences of the N-terminal sequences of all peptides are similar. The different selectivities towards opioid receptors have been interpreted in terms of charge effects in the interaction with the membrane and at the receptor site and of hydrophobicity of the C-terminal part, when structured in a folded conformation. |
| doi_str_mv | 10.1016/0006-291X(90)90375-W |
| format | Article |
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2, recently isolated from the skin of
Phyllomedusa bicolor. Its enormous selectivity towards the δ opioid receptor and the similarity of the conformation of the N-terminal part of the sequence with that of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH
2), a μ selective peptide, prompted the synthesis, biological evaluation and comparative conformational study of four analogs. A
1H-NMR study showed that the conformational preferences of the N-terminal sequences of all peptides are similar. The different selectivities towards opioid receptors have been interpreted in terms of charge effects in the interaction with the membrane and at the receptor site and of hydrophobicity of the C-terminal part, when structured in a folded conformation.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(90)90375-W</identifier><identifier>PMID: 2162669</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Binding, Competitive ; Biological and medical sciences ; Brain - metabolism ; Cell Membrane - metabolism ; Cell receptors ; Cell structures and functions ; deltorphin I ; Fundamental and applied biological sciences. Psychology ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular and cellular biology ; Molecular Sequence Data ; Neuropeptide receptors ; Oligopeptides - chemical synthesis ; Oligopeptides - pharmacology ; Phyllomedusa bicolor ; Protein Conformation ; Rats ; Receptors, Opioid - drug effects ; Receptors, Opioid - metabolism ; Receptors, Opioid, delta ; Receptors, Opioid, mu ; Structure-Activity Relationship</subject><ispartof>Biochemical and biophysical research communications, 1990-06, Vol.169 (2), p.617-622</ispartof><rights>1990</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c418t-47a7d81725254dd98aae48e15eda12bd3c42fdc6a3c483468a5bed40309c0cb83</citedby><cites>FETCH-LOGICAL-c418t-47a7d81725254dd98aae48e15eda12bd3c42fdc6a3c483468a5bed40309c0cb83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(90)90375-W$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19480501$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2162669$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Balboni, G.</creatorcontrib><creatorcontrib>Marastoni, M.</creatorcontrib><creatorcontrib>Picone, D.</creatorcontrib><creatorcontrib>Salvadori, S.</creatorcontrib><creatorcontrib>Tancredi, T.</creatorcontrib><creatorcontrib>Temussi, P.A.</creatorcontrib><creatorcontrib>Tomatis, R.</creatorcontrib><title>New features of the δ opioid receptor: Conformational properties of deltorphin I analogues</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Deltorphin I is an opioid peptide of sequence H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH
2, recently isolated from the skin of
Phyllomedusa bicolor. Its enormous selectivity towards the δ opioid receptor and the similarity of the conformation of the N-terminal part of the sequence with that of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH
2), a μ selective peptide, prompted the synthesis, biological evaluation and comparative conformational study of four analogs. A
1H-NMR study showed that the conformational preferences of the N-terminal sequences of all peptides are similar. The different selectivities towards opioid receptors have been interpreted in terms of charge effects in the interaction with the membrane and at the receptor site and of hydrophobicity of the C-terminal part, when structured in a folded conformation.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Brain - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>deltorphin I</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Neuropeptide receptors</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - pharmacology</subject><subject>Phyllomedusa bicolor</subject><subject>Protein Conformation</subject><subject>Rats</subject><subject>Receptors, Opioid - drug effects</subject><subject>Receptors, Opioid - metabolism</subject><subject>Receptors, Opioid, delta</subject><subject>Receptors, Opioid, mu</subject><subject>Structure-Activity Relationship</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdFqFDEUhoModa2-gUJuLPZi9JyZTCbpRaEsVgul3igVvAjZ5IyNzE6myazie_kcPlOz7lLv9CqB8_1_Dl8Ye47wGgHlGwCQVa3x8ysNxxqarq2uH7AFgoaqRhAP2eIeecye5PwNAFFIfcAOapS1lHrBvlzRD96TnTeJMo89n2-I__7F4xRi8DyRo2mO6YQv49jHtLZziKMd-JTiRGkOu5CnoUDTTRj5BbdlHr9uKD9lj3o7ZHq2Pw_Zp_O3H5fvq8sP7y6WZ5eVE6jmSnS28wq7uq1b4b1W1pJQhC15i_XKN07UvXfSlotqhFS2XZEX0IB24FaqOWRHu96y1G15dzbrkB0Ngx0pbrLptBISFPwXxLYDFCgLKHagSzHnRL2ZUljb9NMgmK18szVrtmaNBvNHvrkusRf7_s1qTf4-tLdd5i_3c5udHfpkRxfy324tFLSAhTvdcVSsfQ-UTHaBRkc-lA-ZjY_h34vcAebQojE</recordid><startdate>19900615</startdate><enddate>19900615</enddate><creator>Balboni, G.</creator><creator>Marastoni, M.</creator><creator>Picone, D.</creator><creator>Salvadori, S.</creator><creator>Tancredi, T.</creator><creator>Temussi, P.A.</creator><creator>Tomatis, R.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19900615</creationdate><title>New features of the δ opioid receptor: Conformational properties of deltorphin I analogues</title><author>Balboni, G. ; Marastoni, M. ; Picone, D. ; Salvadori, S. ; Tancredi, T. ; Temussi, P.A. ; Tomatis, R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-47a7d81725254dd98aae48e15eda12bd3c42fdc6a3c483468a5bed40309c0cb83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Brain - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>deltorphin I</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Neuropeptide receptors</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - pharmacology</topic><topic>Phyllomedusa bicolor</topic><topic>Protein Conformation</topic><topic>Rats</topic><topic>Receptors, Opioid - drug effects</topic><topic>Receptors, Opioid - metabolism</topic><topic>Receptors, Opioid, delta</topic><topic>Receptors, Opioid, mu</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Balboni, G.</creatorcontrib><creatorcontrib>Marastoni, M.</creatorcontrib><creatorcontrib>Picone, D.</creatorcontrib><creatorcontrib>Salvadori, S.</creatorcontrib><creatorcontrib>Tancredi, T.</creatorcontrib><creatorcontrib>Temussi, P.A.</creatorcontrib><creatorcontrib>Tomatis, R.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Balboni, G.</au><au>Marastoni, M.</au><au>Picone, D.</au><au>Salvadori, S.</au><au>Tancredi, T.</au><au>Temussi, P.A.</au><au>Tomatis, R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New features of the δ opioid receptor: Conformational properties of deltorphin I analogues</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1990-06-15</date><risdate>1990</risdate><volume>169</volume><issue>2</issue><spage>617</spage><epage>622</epage><pages>617-622</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>Deltorphin I is an opioid peptide of sequence H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH
2, recently isolated from the skin of
Phyllomedusa bicolor. Its enormous selectivity towards the δ opioid receptor and the similarity of the conformation of the N-terminal part of the sequence with that of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH
2), a μ selective peptide, prompted the synthesis, biological evaluation and comparative conformational study of four analogs. A
1H-NMR study showed that the conformational preferences of the N-terminal sequences of all peptides are similar. The different selectivities towards opioid receptors have been interpreted in terms of charge effects in the interaction with the membrane and at the receptor site and of hydrophobicity of the C-terminal part, when structured in a folded conformation.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2162669</pmid><doi>10.1016/0006-291X(90)90375-W</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1990-06, Vol.169 (2), p.617-622 |
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| subjects | Amino Acid Sequence Animals Binding, Competitive Biological and medical sciences Brain - metabolism Cell Membrane - metabolism Cell receptors Cell structures and functions deltorphin I Fundamental and applied biological sciences. Psychology Magnetic Resonance Spectroscopy Models, Molecular Molecular and cellular biology Molecular Sequence Data Neuropeptide receptors Oligopeptides - chemical synthesis Oligopeptides - pharmacology Phyllomedusa bicolor Protein Conformation Rats Receptors, Opioid - drug effects Receptors, Opioid - metabolism Receptors, Opioid, delta Receptors, Opioid, mu Structure-Activity Relationship |
| title | New features of the δ opioid receptor: Conformational properties of deltorphin I analogues |
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