Conformation and aggregation of melittin: dependence of pH and concentration
Melittin, a 26-residue peptide from bee venom, is transformed from a largely random to a largely alpha-helical conformation at elevated pH. At 3 x 10(-5) M melittin, circular dichroism spectra show a transition with a pK near 9.6. At 8 x 10(-5) M, two approximately equal transitions occur with pKs a...
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| Veröffentlicht in: | Biochemistry (Easton) 1982-02, Vol.21 (3), p.461-465 |
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| container_title | Biochemistry (Easton) |
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| creator | Bello, Jake Bello, Helene R Granados, Edward |
| description | Melittin, a 26-residue peptide from bee venom, is transformed from a largely random to a largely alpha-helical conformation at elevated pH. At 3 x 10(-5) M melittin, circular dichroism spectra show a transition with a pK near 9.6. At 8 x 10(-5) M, two approximately equal transitions occur with pKs at 7.2 and 9.6. At 6 x 10(-4) M, a single transition is seen with a pK of 6.8, followed by a more gradual increase to at least pH 11. The transitions near pH 7 presumably arise from deprotonation of the alpha-amino group. When the amino groups are acetylated or succinylated, a 60% alpha-helical conformation is adopted at neutral or low pH. The acylated melittins form more stable oligomers than does native melittin. |
| doi_str_mv | 10.1021/bi00532a007 |
| format | Article |
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At 3 x 10(-5) M melittin, circular dichroism spectra show a transition with a pK near 9.6. At 8 x 10(-5) M, two approximately equal transitions occur with pKs at 7.2 and 9.6. At 6 x 10(-4) M, a single transition is seen with a pK of 6.8, followed by a more gradual increase to at least pH 11. The transitions near pH 7 presumably arise from deprotonation of the alpha-amino group. When the amino groups are acetylated or succinylated, a 60% alpha-helical conformation is adopted at neutral or low pH. The acylated melittins form more stable oligomers than does native melittin.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00532a007</identifier><identifier>PMID: 7066299</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Apis mellifera ; Bee Venoms ; C.D ; Circular Dichroism ; conformation ; Hydrogen-Ion Concentration ; Kinetics ; Macromolecular Substances ; Melitten ; melittin ; Molecular Weight ; Protein Conformation ; venom</subject><ispartof>Biochemistry (Easton), 1982-02, Vol.21 (3), p.461-465</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a451t-a4256054e7a85b7a1b85dc0dbcd6db08695c7f946a0f985eb0a9475bc5387c273</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00532a007$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00532a007$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2763,27074,27922,27923,56736,56786</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7066299$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bello, Jake</creatorcontrib><creatorcontrib>Bello, Helene R</creatorcontrib><creatorcontrib>Granados, Edward</creatorcontrib><title>Conformation and aggregation of melittin: dependence of pH and concentration</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Melittin, a 26-residue peptide from bee venom, is transformed from a largely random to a largely alpha-helical conformation at elevated pH. At 3 x 10(-5) M melittin, circular dichroism spectra show a transition with a pK near 9.6. At 8 x 10(-5) M, two approximately equal transitions occur with pKs at 7.2 and 9.6. At 6 x 10(-4) M, a single transition is seen with a pK of 6.8, followed by a more gradual increase to at least pH 11. The transitions near pH 7 presumably arise from deprotonation of the alpha-amino group. When the amino groups are acetylated or succinylated, a 60% alpha-helical conformation is adopted at neutral or low pH. The acylated melittins form more stable oligomers than does native melittin.</description><subject>Apis mellifera</subject><subject>Bee Venoms</subject><subject>C.D</subject><subject>Circular Dichroism</subject><subject>conformation</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Melitten</subject><subject>melittin</subject><subject>Molecular Weight</subject><subject>Protein Conformation</subject><subject>venom</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1982</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1LwzAYh4MoOj9OnoWd9CDVN22TNN7ccJtQ_MCPa0jTdFTXZCYt6H9vtg7xIHhJ-OX35H3hQegYwwWGGF8WNQBJYgnAttAAkxiilHOyjQYAQKOYU9hD-96_hZgCS3fRLgNKY84HKB9bU1nXyLa2ZihNOZTzudPzPttq2OhF3ba1uRqWeqlNqY3Sq_flbE0rG7Jp3Zo_RDuVXHh9tLkP0Mvk5nk8i_L76e34Oo9kSnAbzphQIKlmMiMFk7jISKmgLFRJywIyyoliFU-phIpnRBcgecpIoUiSMRWz5ACd9nOXzn502reiqb3Si4U02nZesCR8ywj9F8QkxSs9ATzvQeWs905XYunqRrovgUGsJItfkgN9shnbFY0uf9iN1dBHfV_7Vn_-1NK9C8oSRsTzw5PIR5PpKL97FY-BP-t5qbx4s50zwd6fm78BEe-SQQ</recordid><startdate>19820201</startdate><enddate>19820201</enddate><creator>Bello, Jake</creator><creator>Bello, Helene R</creator><creator>Granados, Edward</creator><general>American Chemical Society</general><scope>BSCLL</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>7QL</scope><scope>7SS</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19820201</creationdate><title>Conformation and aggregation of melittin: dependence of pH and concentration</title><author>Bello, Jake ; Bello, Helene R ; Granados, Edward</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a451t-a4256054e7a85b7a1b85dc0dbcd6db08695c7f946a0f985eb0a9475bc5387c273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1982</creationdate><topic>Apis mellifera</topic><topic>Bee Venoms</topic><topic>C.D</topic><topic>Circular Dichroism</topic><topic>conformation</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Melitten</topic><topic>melittin</topic><topic>Molecular Weight</topic><topic>Protein Conformation</topic><topic>venom</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bello, Jake</creatorcontrib><creatorcontrib>Bello, Helene R</creatorcontrib><creatorcontrib>Granados, Edward</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bello, Jake</au><au>Bello, Helene R</au><au>Granados, Edward</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformation and aggregation of melittin: dependence of pH and concentration</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1982-02-01</date><risdate>1982</risdate><volume>21</volume><issue>3</issue><spage>461</spage><epage>465</epage><pages>461-465</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Melittin, a 26-residue peptide from bee venom, is transformed from a largely random to a largely alpha-helical conformation at elevated pH. At 3 x 10(-5) M melittin, circular dichroism spectra show a transition with a pK near 9.6. At 8 x 10(-5) M, two approximately equal transitions occur with pKs at 7.2 and 9.6. At 6 x 10(-4) M, a single transition is seen with a pK of 6.8, followed by a more gradual increase to at least pH 11. The transitions near pH 7 presumably arise from deprotonation of the alpha-amino group. When the amino groups are acetylated or succinylated, a 60% alpha-helical conformation is adopted at neutral or low pH. The acylated melittins form more stable oligomers than does native melittin.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>7066299</pmid><doi>10.1021/bi00532a007</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1982-02, Vol.21 (3), p.461-465 |
| issn | 0006-2960 1520-4995 |
| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | Apis mellifera Bee Venoms C.D Circular Dichroism conformation Hydrogen-Ion Concentration Kinetics Macromolecular Substances Melitten melittin Molecular Weight Protein Conformation venom |
| title | Conformation and aggregation of melittin: dependence of pH and concentration |
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