Analogues of N-hydroxycinnamoylphenalkylamides as inhibitors of human melanocyte-tyrosinase
Amides obtained by coupling caffeic acid, ferulic acid, p-hydroxycinnamoic acid, and analogues with substituted phenylalkylamines were evaluated as inhibitors of the human melanocyte-tyrosinase. The most active compounds induce a complete enzyme-inactivation at 100 μM. At the latter concentration, k...
Gespeichert in:
| Veröffentlicht in: | Bioorganic & medicinal chemistry letters 2006-04, Vol.16 (8), p.2252-2255 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2255 |
|---|---|
| container_issue | 8 |
| container_start_page | 2252 |
| container_title | Bioorganic & medicinal chemistry letters |
| container_volume | 16 |
| creator | Okombi, Sabrina Rival, Delphine Bonnet, Sébastien Mariotte, Anne-Marie Perrier, Eric Boumendjel, Ahcène |
| description | Amides obtained by coupling caffeic acid, ferulic acid,
p-hydroxycinnamoic acid, and analogues with substituted phenylalkylamines were evaluated as inhibitors of the human melanocyte-tyrosinase. The most active compounds induce a complete enzyme-inactivation at 100
μM. At the latter concentration, kojic acid, used as a reference, was inactive.
Melanin play a major role in human skin protection and their biosynthesis is vital. Due to their color, they contribute to the skin pigmentation. Tyrosinase is a key enzyme involved in the first stage of melanin synthesis, catalyzing the transformation of tyrosine to
l-dopaquinone. The aim of the present study was to study molecules able to inhibit melanin synthesis through inhibition of tyrosinase and their potential use in treating pigmentation-related disorders. We targeted amides obtained from coupling
p-hydroxycinnamic acid derivatives with phenylalkylamines. The biological activity was evaluated on human melanocytes by an assay which measures tyrosine-catalyzed
l-Dopa oxidation. The most active amides were:
trans-
N-caffeoyltyramine,
N-dihydrocaffeoyltyramine, and
trans-
N-dihydro-
p-hydroxycinnamoyltyramine which induce complete inhibition at 0.1
mM. At the latter concentration, kojic acid, which was used as the reference inhibitor, was inactive. |
| doi_str_mv | 10.1016/j.bmcl.2006.01.022 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67731336</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0960894X06000424</els_id><sourcerecordid>17161161</sourcerecordid><originalsourceid>FETCH-LOGICAL-c415t-f3d827c0944aa48119ff40a138a63def69e4784db5571147732743a60dfc6dd73</originalsourceid><addsrcrecordid>eNqFkE2LFDEQhoMo7uzqH_Agc9Fbt1Wd6qQbvCzL6gqLXhQEDyGTDydjd2dMesT-92acgb0pFNTleV-qHsZeINQIKN7s6s1ohroBEDVgDU3ziK2QBFWcoH3MVtALqLqevl6wy5x3AEhA9JRdoCBqZC9W7Nv1pIf4_eDyOvr1x2q72BR_LyZMkx7jMuy3rgA_lkGPwRZI53WYtmET5pj-RraHUU_r0Q16imaZXTUvKeYw6eyesSdeD9k9P-8r9uXd7eebu-r-0_sPN9f3lSFs58pz2zXSQE-kNXWIvfcEGnmnBbfOi96R7Mhu2lYikpS8kcS1AOuNsFbyK_b61LtP8Wf5ZFZjyMYN5SQXD1mJEkHOxX9BlCiwTAGbE2jKLzk5r_YpjDotCkEd3audOrpXR_cKUBX3JfTy3H7YjM4-RM6yC_DqDOhs9OCTnkzID5xsZQcIhXt74lyR9iu4pLIJbjLOhuTMrGwM_7rjD-Lwo1k</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17161161</pqid></control><display><type>article</type><title>Analogues of N-hydroxycinnamoylphenalkylamides as inhibitors of human melanocyte-tyrosinase</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Okombi, Sabrina ; Rival, Delphine ; Bonnet, Sébastien ; Mariotte, Anne-Marie ; Perrier, Eric ; Boumendjel, Ahcène</creator><creatorcontrib>Okombi, Sabrina ; Rival, Delphine ; Bonnet, Sébastien ; Mariotte, Anne-Marie ; Perrier, Eric ; Boumendjel, Ahcène</creatorcontrib><description>Amides obtained by coupling caffeic acid, ferulic acid,
p-hydroxycinnamoic acid, and analogues with substituted phenylalkylamines were evaluated as inhibitors of the human melanocyte-tyrosinase. The most active compounds induce a complete enzyme-inactivation at 100
μM. At the latter concentration, kojic acid, used as a reference, was inactive.
Melanin play a major role in human skin protection and their biosynthesis is vital. Due to their color, they contribute to the skin pigmentation. Tyrosinase is a key enzyme involved in the first stage of melanin synthesis, catalyzing the transformation of tyrosine to
l-dopaquinone. The aim of the present study was to study molecules able to inhibit melanin synthesis through inhibition of tyrosinase and their potential use in treating pigmentation-related disorders. We targeted amides obtained from coupling
p-hydroxycinnamic acid derivatives with phenylalkylamines. The biological activity was evaluated on human melanocytes by an assay which measures tyrosine-catalyzed
l-Dopa oxidation. The most active amides were:
trans-
N-caffeoyltyramine,
N-dihydrocaffeoyltyramine, and
trans-
N-dihydro-
p-hydroxycinnamoyltyramine which induce complete inhibition at 0.1
mM. At the latter concentration, kojic acid, which was used as the reference inhibitor, was inactive.</description><identifier>ISSN: 0960-894X</identifier><identifier>EISSN: 1464-3405</identifier><identifier>DOI: 10.1016/j.bmcl.2006.01.022</identifier><identifier>PMID: 16442796</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amides ; Amides - chemical synthesis ; Amides - pharmacology ; Benzoquinones - metabolism ; Biological and medical sciences ; Caffeic Acids - chemical synthesis ; Caffeic Acids - pharmacology ; Catalysis ; Cells, Cultured ; Dihydroxyphenylalanine - analogs & derivatives ; Dihydroxyphenylalanine - metabolism ; Enzyme Inhibitors - chemical synthesis ; Enzyme Inhibitors - pharmacology ; Humans ; Levodopa - pharmacology ; Medical sciences ; Melanin ; Melanins - antagonists & inhibitors ; Melanins - biosynthesis ; Melanocytes - drug effects ; Melanocytes - enzymology ; Monophenol Monooxygenase - antagonists & inhibitors ; N-Hydroxycinnamic acid analogues ; Oxidation-Reduction ; Pharmacology. Drug treatments ; Phenylalkylamines ; Pigmentation Disorders - drug therapy ; Pyrones - pharmacology ; Skin - drug effects ; Skin, nail, hair, dermoskeleton ; Structure-Activity Relationship ; Tyramine - analogs & derivatives ; Tyramine - chemical synthesis ; Tyramine - pharmacology ; Tyrosinase inhibitors ; Tyrosine - metabolism</subject><ispartof>Bioorganic & medicinal chemistry letters, 2006-04, Vol.16 (8), p.2252-2255</ispartof><rights>2006 Elsevier Ltd</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c415t-f3d827c0944aa48119ff40a138a63def69e4784db5571147732743a60dfc6dd73</citedby><cites>FETCH-LOGICAL-c415t-f3d827c0944aa48119ff40a138a63def69e4784db5571147732743a60dfc6dd73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bmcl.2006.01.022$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17578010$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16442796$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okombi, Sabrina</creatorcontrib><creatorcontrib>Rival, Delphine</creatorcontrib><creatorcontrib>Bonnet, Sébastien</creatorcontrib><creatorcontrib>Mariotte, Anne-Marie</creatorcontrib><creatorcontrib>Perrier, Eric</creatorcontrib><creatorcontrib>Boumendjel, Ahcène</creatorcontrib><title>Analogues of N-hydroxycinnamoylphenalkylamides as inhibitors of human melanocyte-tyrosinase</title><title>Bioorganic & medicinal chemistry letters</title><addtitle>Bioorg Med Chem Lett</addtitle><description>Amides obtained by coupling caffeic acid, ferulic acid,
p-hydroxycinnamoic acid, and analogues with substituted phenylalkylamines were evaluated as inhibitors of the human melanocyte-tyrosinase. The most active compounds induce a complete enzyme-inactivation at 100
μM. At the latter concentration, kojic acid, used as a reference, was inactive.
Melanin play a major role in human skin protection and their biosynthesis is vital. Due to their color, they contribute to the skin pigmentation. Tyrosinase is a key enzyme involved in the first stage of melanin synthesis, catalyzing the transformation of tyrosine to
l-dopaquinone. The aim of the present study was to study molecules able to inhibit melanin synthesis through inhibition of tyrosinase and their potential use in treating pigmentation-related disorders. We targeted amides obtained from coupling
p-hydroxycinnamic acid derivatives with phenylalkylamines. The biological activity was evaluated on human melanocytes by an assay which measures tyrosine-catalyzed
l-Dopa oxidation. The most active amides were:
trans-
N-caffeoyltyramine,
N-dihydrocaffeoyltyramine, and
trans-
N-dihydro-
p-hydroxycinnamoyltyramine which induce complete inhibition at 0.1
mM. At the latter concentration, kojic acid, which was used as the reference inhibitor, was inactive.</description><subject>Amides</subject><subject>Amides - chemical synthesis</subject><subject>Amides - pharmacology</subject><subject>Benzoquinones - metabolism</subject><subject>Biological and medical sciences</subject><subject>Caffeic Acids - chemical synthesis</subject><subject>Caffeic Acids - pharmacology</subject><subject>Catalysis</subject><subject>Cells, Cultured</subject><subject>Dihydroxyphenylalanine - analogs & derivatives</subject><subject>Dihydroxyphenylalanine - metabolism</subject><subject>Enzyme Inhibitors - chemical synthesis</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Humans</subject><subject>Levodopa - pharmacology</subject><subject>Medical sciences</subject><subject>Melanin</subject><subject>Melanins - antagonists & inhibitors</subject><subject>Melanins - biosynthesis</subject><subject>Melanocytes - drug effects</subject><subject>Melanocytes - enzymology</subject><subject>Monophenol Monooxygenase - antagonists & inhibitors</subject><subject>N-Hydroxycinnamic acid analogues</subject><subject>Oxidation-Reduction</subject><subject>Pharmacology. Drug treatments</subject><subject>Phenylalkylamines</subject><subject>Pigmentation Disorders - drug therapy</subject><subject>Pyrones - pharmacology</subject><subject>Skin - drug effects</subject><subject>Skin, nail, hair, dermoskeleton</subject><subject>Structure-Activity Relationship</subject><subject>Tyramine - analogs & derivatives</subject><subject>Tyramine - chemical synthesis</subject><subject>Tyramine - pharmacology</subject><subject>Tyrosinase inhibitors</subject><subject>Tyrosine - metabolism</subject><issn>0960-894X</issn><issn>1464-3405</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2LFDEQhoMo7uzqH_Agc9Fbt1Wd6qQbvCzL6gqLXhQEDyGTDydjd2dMesT-92acgb0pFNTleV-qHsZeINQIKN7s6s1ohroBEDVgDU3ziK2QBFWcoH3MVtALqLqevl6wy5x3AEhA9JRdoCBqZC9W7Nv1pIf4_eDyOvr1x2q72BR_LyZMkx7jMuy3rgA_lkGPwRZI53WYtmET5pj-RraHUU_r0Q16imaZXTUvKeYw6eyesSdeD9k9P-8r9uXd7eebu-r-0_sPN9f3lSFs58pz2zXSQE-kNXWIvfcEGnmnBbfOi96R7Mhu2lYikpS8kcS1AOuNsFbyK_b61LtP8Wf5ZFZjyMYN5SQXD1mJEkHOxX9BlCiwTAGbE2jKLzk5r_YpjDotCkEd3audOrpXR_cKUBX3JfTy3H7YjM4-RM6yC_DqDOhs9OCTnkzID5xsZQcIhXt74lyR9iu4pLIJbjLOhuTMrGwM_7rjD-Lwo1k</recordid><startdate>20060415</startdate><enddate>20060415</enddate><creator>Okombi, Sabrina</creator><creator>Rival, Delphine</creator><creator>Bonnet, Sébastien</creator><creator>Mariotte, Anne-Marie</creator><creator>Perrier, Eric</creator><creator>Boumendjel, Ahcène</creator><general>Elsevier Ltd</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20060415</creationdate><title>Analogues of N-hydroxycinnamoylphenalkylamides as inhibitors of human melanocyte-tyrosinase</title><author>Okombi, Sabrina ; Rival, Delphine ; Bonnet, Sébastien ; Mariotte, Anne-Marie ; Perrier, Eric ; Boumendjel, Ahcène</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-f3d827c0944aa48119ff40a138a63def69e4784db5571147732743a60dfc6dd73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amides</topic><topic>Amides - chemical synthesis</topic><topic>Amides - pharmacology</topic><topic>Benzoquinones - metabolism</topic><topic>Biological and medical sciences</topic><topic>Caffeic Acids - chemical synthesis</topic><topic>Caffeic Acids - pharmacology</topic><topic>Catalysis</topic><topic>Cells, Cultured</topic><topic>Dihydroxyphenylalanine - analogs & derivatives</topic><topic>Dihydroxyphenylalanine - metabolism</topic><topic>Enzyme Inhibitors - chemical synthesis</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Humans</topic><topic>Levodopa - pharmacology</topic><topic>Medical sciences</topic><topic>Melanin</topic><topic>Melanins - antagonists & inhibitors</topic><topic>Melanins - biosynthesis</topic><topic>Melanocytes - drug effects</topic><topic>Melanocytes - enzymology</topic><topic>Monophenol Monooxygenase - antagonists & inhibitors</topic><topic>N-Hydroxycinnamic acid analogues</topic><topic>Oxidation-Reduction</topic><topic>Pharmacology. Drug treatments</topic><topic>Phenylalkylamines</topic><topic>Pigmentation Disorders - drug therapy</topic><topic>Pyrones - pharmacology</topic><topic>Skin - drug effects</topic><topic>Skin, nail, hair, dermoskeleton</topic><topic>Structure-Activity Relationship</topic><topic>Tyramine - analogs & derivatives</topic><topic>Tyramine - chemical synthesis</topic><topic>Tyramine - pharmacology</topic><topic>Tyrosinase inhibitors</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okombi, Sabrina</creatorcontrib><creatorcontrib>Rival, Delphine</creatorcontrib><creatorcontrib>Bonnet, Sébastien</creatorcontrib><creatorcontrib>Mariotte, Anne-Marie</creatorcontrib><creatorcontrib>Perrier, Eric</creatorcontrib><creatorcontrib>Boumendjel, Ahcène</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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Okombi, Sabrina</au><au>Rival, Delphine</au><au>Bonnet, Sébastien</au><au>Mariotte, Anne-Marie</au><au>Perrier, Eric</au><au>Boumendjel, Ahcène</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analogues of N-hydroxycinnamoylphenalkylamides as inhibitors of human melanocyte-tyrosinase</atitle><jtitle>Bioorganic & medicinal chemistry letters</jtitle><addtitle>Bioorg Med Chem Lett</addtitle><date>2006-04-15</date><risdate>2006</risdate><volume>16</volume><issue>8</issue><spage>2252</spage><epage>2255</epage><pages>2252-2255</pages><issn>0960-894X</issn><eissn>1464-3405</eissn><abstract>Amides obtained by coupling caffeic acid, ferulic acid,
p-hydroxycinnamoic acid, and analogues with substituted phenylalkylamines were evaluated as inhibitors of the human melanocyte-tyrosinase. The most active compounds induce a complete enzyme-inactivation at 100
μM. At the latter concentration, kojic acid, used as a reference, was inactive.
Melanin play a major role in human skin protection and their biosynthesis is vital. Due to their color, they contribute to the skin pigmentation. Tyrosinase is a key enzyme involved in the first stage of melanin synthesis, catalyzing the transformation of tyrosine to
l-dopaquinone. The aim of the present study was to study molecules able to inhibit melanin synthesis through inhibition of tyrosinase and their potential use in treating pigmentation-related disorders. We targeted amides obtained from coupling
p-hydroxycinnamic acid derivatives with phenylalkylamines. The biological activity was evaluated on human melanocytes by an assay which measures tyrosine-catalyzed
l-Dopa oxidation. The most active amides were:
trans-
N-caffeoyltyramine,
N-dihydrocaffeoyltyramine, and
trans-
N-dihydro-
p-hydroxycinnamoyltyramine which induce complete inhibition at 0.1
mM. At the latter concentration, kojic acid, which was used as the reference inhibitor, was inactive.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>16442796</pmid><doi>10.1016/j.bmcl.2006.01.022</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0960-894X |
| ispartof | Bioorganic & medicinal chemistry letters, 2006-04, Vol.16 (8), p.2252-2255 |
| issn | 0960-894X 1464-3405 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_67731336 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amides Amides - chemical synthesis Amides - pharmacology Benzoquinones - metabolism Biological and medical sciences Caffeic Acids - chemical synthesis Caffeic Acids - pharmacology Catalysis Cells, Cultured Dihydroxyphenylalanine - analogs & derivatives Dihydroxyphenylalanine - metabolism Enzyme Inhibitors - chemical synthesis Enzyme Inhibitors - pharmacology Humans Levodopa - pharmacology Medical sciences Melanin Melanins - antagonists & inhibitors Melanins - biosynthesis Melanocytes - drug effects Melanocytes - enzymology Monophenol Monooxygenase - antagonists & inhibitors N-Hydroxycinnamic acid analogues Oxidation-Reduction Pharmacology. Drug treatments Phenylalkylamines Pigmentation Disorders - drug therapy Pyrones - pharmacology Skin - drug effects Skin, nail, hair, dermoskeleton Structure-Activity Relationship Tyramine - analogs & derivatives Tyramine - chemical synthesis Tyramine - pharmacology Tyrosinase inhibitors Tyrosine - metabolism |
| title | Analogues of N-hydroxycinnamoylphenalkylamides as inhibitors of human melanocyte-tyrosinase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T20%3A30%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Analogues%20of%20N-hydroxycinnamoylphenalkylamides%20as%20inhibitors%20of%20human%20melanocyte-tyrosinase&rft.jtitle=Bioorganic%20&%20medicinal%20chemistry%20letters&rft.au=Okombi,%20Sabrina&rft.date=2006-04-15&rft.volume=16&rft.issue=8&rft.spage=2252&rft.epage=2255&rft.pages=2252-2255&rft.issn=0960-894X&rft.eissn=1464-3405&rft_id=info:doi/10.1016/j.bmcl.2006.01.022&rft_dat=%3Cproquest_cross%3E17161161%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17161161&rft_id=info:pmid/16442796&rft_els_id=S0960894X06000424&rfr_iscdi=true |