Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin
| ISSN: |
1573-4943
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|---|---|
| Keywords: |
insulin analogue ; peptide synthesis ; receptor binding assay ; radioimmunoassay ; lipogenesis assay
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| Source: |
Springer Online Journal Archives 1860-2000
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| Topics: |
Chemistry and Pharmacology
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| Notes: |
Abstract As part of our aim to study the conformation of insulin in solution by time-resolved fluorescence spectroscopy, we have synthesized the analogue [19-Tryptophan-A]insulin. In this compound, the tyrosine residue at position 19 of the A-chain of insulin, one of the most strongly conserved residues in insulins from various species, is substituted with the strongly fluorescent tryptophan residue. [19-Tryptophan-A]insulin displays 4.1±1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0±2.3% in stimulating lipogenesis in rat adipocytes, and 75.7±4% of the potency of insulin in radioimmunoassay. In connection with our previous work, these data indicate that an aromatic side chain at position A19 of insulin seems necessary but not sufficient for high biological activity. We further conclude that in regard to the immunogenic determinants of insulin, tryptophan in position A19 is an essentially neutral substitution for tyrosine in that position, in sharp contrast to the situation with regard to biological activity.
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798296778341089280 |
|---|---|
| autor | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. |
| autorsonst | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. |
| book_url | http://dx.doi.org/10.1007/BF01025414 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM197815375 |
| issn | 1573-4943 |
| journal_name | The protein journal |
| materialart | 1 |
| notes | Abstract As part of our aim to study the conformation of insulin in solution by time-resolved fluorescence spectroscopy, we have synthesized the analogue [19-Tryptophan-A]insulin. In this compound, the tyrosine residue at position 19 of the A-chain of insulin, one of the most strongly conserved residues in insulins from various species, is substituted with the strongly fluorescent tryptophan residue. [19-Tryptophan-A]insulin displays 4.1±1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0±2.3% in stimulating lipogenesis in rat adipocytes, and 75.7±4% of the potency of insulin in radioimmunoassay. In connection with our previous work, these data indicate that an aromatic side chain at position A19 of insulin seems necessary but not sufficient for high biological activity. We further conclude that in regard to the immunogenic determinants of insulin, tryptophan in position A19 is an essentially neutral substitution for tyrosine in that position, in sharp contrast to the situation with regard to biological activity. |
| package_name | Springer |
| publikationsjahr_anzeige | 1988 |
| publikationsjahr_facette | 1988 |
| publikationsjahr_intervall | 8014:1985-1989 |
| publikationsjahr_sort | 1988 |
| publisher | Springer |
| reference | 7 (1988), S. 55-65 |
| schlagwort | insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay |
| search_space | articles |
| shingle_author_1 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_author_2 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_author_3 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_author_4 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. |
| shingle_catch_all_1 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay Abstract As part of our aim to study the conformation of insulin in solution by time-resolved fluorescence spectroscopy, we have synthesized the analogue [19-Tryptophan-A]insulin. In this compound, the tyrosine residue at position 19 of the A-chain of insulin, one of the most strongly conserved residues in insulins from various species, is substituted with the strongly fluorescent tryptophan residue. [19-Tryptophan-A]insulin displays 4.1±1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0±2.3% in stimulating lipogenesis in rat adipocytes, and 75.7±4% of the potency of insulin in radioimmunoassay. In connection with our previous work, these data indicate that an aromatic side chain at position A19 of insulin seems necessary but not sufficient for high biological activity. We further conclude that in regard to the immunogenic determinants of insulin, tryptophan in position A19 is an essentially neutral substitution for tyrosine in that position, in sharp contrast to the situation with regard to biological activity. 1573-4943 15734943 Springer |
| shingle_catch_all_2 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay Abstract As part of our aim to study the conformation of insulin in solution by time-resolved fluorescence spectroscopy, we have synthesized the analogue [19-Tryptophan-A]insulin. In this compound, the tyrosine residue at position 19 of the A-chain of insulin, one of the most strongly conserved residues in insulins from various species, is substituted with the strongly fluorescent tryptophan residue. [19-Tryptophan-A]insulin displays 4.1±1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0±2.3% in stimulating lipogenesis in rat adipocytes, and 75.7±4% of the potency of insulin in radioimmunoassay. In connection with our previous work, these data indicate that an aromatic side chain at position A19 of insulin seems necessary but not sufficient for high biological activity. We further conclude that in regard to the immunogenic determinants of insulin, tryptophan in position A19 is an essentially neutral substitution for tyrosine in that position, in sharp contrast to the situation with regard to biological activity. 1573-4943 15734943 Springer |
| shingle_catch_all_3 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay Abstract As part of our aim to study the conformation of insulin in solution by time-resolved fluorescence spectroscopy, we have synthesized the analogue [19-Tryptophan-A]insulin. In this compound, the tyrosine residue at position 19 of the A-chain of insulin, one of the most strongly conserved residues in insulins from various species, is substituted with the strongly fluorescent tryptophan residue. [19-Tryptophan-A]insulin displays 4.1±1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0±2.3% in stimulating lipogenesis in rat adipocytes, and 75.7±4% of the potency of insulin in radioimmunoassay. In connection with our previous work, these data indicate that an aromatic side chain at position A19 of insulin seems necessary but not sufficient for high biological activity. We further conclude that in regard to the immunogenic determinants of insulin, tryptophan in position A19 is an essentially neutral substitution for tyrosine in that position, in sharp contrast to the situation with regard to biological activity. 1573-4943 15734943 Springer |
| shingle_catch_all_4 | Ohta, Noriya Burke, G. Thompson Katsoyannis, Panayotis G. Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay insulin analogue peptide synthesis receptor binding assay radioimmunoassay lipogenesis assay Abstract As part of our aim to study the conformation of insulin in solution by time-resolved fluorescence spectroscopy, we have synthesized the analogue [19-Tryptophan-A]insulin. In this compound, the tyrosine residue at position 19 of the A-chain of insulin, one of the most strongly conserved residues in insulins from various species, is substituted with the strongly fluorescent tryptophan residue. [19-Tryptophan-A]insulin displays 4.1±1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0±2.3% in stimulating lipogenesis in rat adipocytes, and 75.7±4% of the potency of insulin in radioimmunoassay. In connection with our previous work, these data indicate that an aromatic side chain at position A19 of insulin seems necessary but not sufficient for high biological activity. We further conclude that in regard to the immunogenic determinants of insulin, tryptophan in position A19 is an essentially neutral substitution for tyrosine in that position, in sharp contrast to the situation with regard to biological activity. 1573-4943 15734943 Springer |
| shingle_title_1 | Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin |
| shingle_title_2 | Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin |
| shingle_title_3 | Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin |
| shingle_title_4 | Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T09:57:29.779Z |
| titel | Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin |
| titel_suche | Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-Tryptophan-A]insulin |
| topic | V |
| uid | nat_lic_papers_NLM197815375 |