Unusually stable helical kink in the antimicrobial peptide — A derivative of gaegurin
The structure of an active analog of the antibacterial peptide gaegurin was investigated by CD and NMR spectroscopy. The NOE connectivities showed that 21 out of 24 residues formed an α-helix despite the presence of a central proline. CD and NMR analysis indicates that the helix is in fast equilibri...
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| Veröffentlicht in: | FEBS letters 1996-09, Vol.392 (3), p.309-312 |
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| creator | Suh, Jeong-Yong Lee, Keun-Hyeung Chi, Seung-Wook Hong, Seong-Yu Choi, Byoung-Wook Moon, Hong-Mo Choi, Byong-Seok |
| description | The structure of an active analog of the antibacterial peptide gaegurin was investigated by CD and NMR spectroscopy. The NOE connectivities showed that 21 out of 24 residues formed an α-helix despite the presence of a central proline. CD and NMR analysis indicates that the helix is in fast equilibrium with random coil. From chemical shift analysis of the amide protons, the distances of hydrogen bonding in the helix were calculated, and manifested obvious periodicity which implied a kink in the middle of the helix. 1D amide proton exchange experiments provided further evidence of an exceptionally stable kink. It is inferred that this kink is important not only to the function of the peptide but also to the early stage of the folding as a nucleation site. |
| doi_str_mv | 10.1016/0014-5793(96)00840-X |
| format | Article |
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The NOE connectivities showed that 21 out of 24 residues formed an α-helix despite the presence of a central proline. CD and NMR analysis indicates that the helix is in fast equilibrium with random coil. From chemical shift analysis of the amide protons, the distances of hydrogen bonding in the helix were calculated, and manifested obvious periodicity which implied a kink in the middle of the helix. 1D amide proton exchange experiments provided further evidence of an exceptionally stable kink. 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The NOE connectivities showed that 21 out of 24 residues formed an α-helix despite the presence of a central proline. CD and NMR analysis indicates that the helix is in fast equilibrium with random coil. From chemical shift analysis of the amide protons, the distances of hydrogen bonding in the helix were calculated, and manifested obvious periodicity which implied a kink in the middle of the helix. 1D amide proton exchange experiments provided further evidence of an exceptionally stable kink. It is inferred that this kink is important not only to the function of the peptide but also to the early stage of the folding as a nucleation site.</description><subject>9-fluorenylmethyloxycarbonyl</subject><subject>Anti-Infective Agents - chemistry</subject><subject>Circular Dichroism</subject><subject>Fmoc</subject><subject>Gaegurin</subject><subject>Hydrogen Bonding</subject><subject>Kink</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>NMR</subject><subject>NOE</subject><subject>NOESY</subject><subject>nuclear Overhauser enhancement</subject><subject>nuclear Overhauser enhancement spectroscopy</subject><subject>one-dimensional</subject><subject>Peptides - chemistry</subject><subject>Peptides - pharmacology</subject><subject>Protein Conformation</subject><subject>reverse phase-high performance liquid chromatography</subject><subject>RP-HPLC</subject><subject>Structure-Activity Relationship</subject><subject>TOCSY</subject><subject>total correlation spectroscopy</subject><subject>α-Helix</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM9u1DAQxi1EVbaFNwDJJ0QPKXbs-M8FqVRdWqkSFyr2Zjn2uDX1JoudLNobD8ET8iQk7KpHxGk0833z2fND6DUl55RQ8Z4QyqtGavZOizNCFCfV6hlaUCVZxbhQz9HiyfICnZTyjUy9ovoYHSspuRJ6gb7edWMZbUo7XAbbJsAPkKKzCT_G7hHHDg8PgG03xHV0uW_jpGxgM0QP-PfPX_gCe8hxa4e4BdwHfG_hfsyxe4mOgk0FXh3qKbpbXn25vK5uP3-6uby4rVzD5KrSQbWqburghRXUUsuFtE3QXvnWq8C4dhqsC41oGRO2ZpS3wJ0OAJJIrdkpervP3eT--whlMOtYHKRkO-jHYqSqVSNoMxn53jhdUUqGYDY5rm3eGUrMzNPMsMwMy-i5mXia1bT25pA_tmvwT0sHgJO-3Os_YoLdf2Wa5dXHehbmuRZ_p_NDH_ZBMNHaRsimuAidAx8zuMH4Pv77p38A83eaCg</recordid><startdate>19960902</startdate><enddate>19960902</enddate><creator>Suh, Jeong-Yong</creator><creator>Lee, Keun-Hyeung</creator><creator>Chi, Seung-Wook</creator><creator>Hong, Seong-Yu</creator><creator>Choi, Byoung-Wook</creator><creator>Moon, Hong-Mo</creator><creator>Choi, Byong-Seok</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>19960902</creationdate><title>Unusually stable helical kink in the antimicrobial peptide — A derivative of gaegurin</title><author>Suh, Jeong-Yong ; Lee, Keun-Hyeung ; Chi, Seung-Wook ; Hong, Seong-Yu ; Choi, Byoung-Wook ; Moon, Hong-Mo ; Choi, Byong-Seok</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c537X-9f8b8252fd6a61a1a467a5f9d8dbd8f349c9eacf56b336a2314be4c9fee707993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>9-fluorenylmethyloxycarbonyl</topic><topic>Anti-Infective Agents - chemistry</topic><topic>Circular Dichroism</topic><topic>Fmoc</topic><topic>Gaegurin</topic><topic>Hydrogen Bonding</topic><topic>Kink</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>NMR</topic><topic>NOE</topic><topic>NOESY</topic><topic>nuclear Overhauser enhancement</topic><topic>nuclear Overhauser enhancement spectroscopy</topic><topic>one-dimensional</topic><topic>Peptides - chemistry</topic><topic>Peptides - pharmacology</topic><topic>Protein Conformation</topic><topic>reverse phase-high performance liquid chromatography</topic><topic>RP-HPLC</topic><topic>Structure-Activity Relationship</topic><topic>TOCSY</topic><topic>total correlation spectroscopy</topic><topic>α-Helix</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Suh, Jeong-Yong</creatorcontrib><creatorcontrib>Lee, Keun-Hyeung</creatorcontrib><creatorcontrib>Chi, Seung-Wook</creatorcontrib><creatorcontrib>Hong, Seong-Yu</creatorcontrib><creatorcontrib>Choi, Byoung-Wook</creatorcontrib><creatorcontrib>Moon, Hong-Mo</creatorcontrib><creatorcontrib>Choi, Byong-Seok</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Suh, Jeong-Yong</au><au>Lee, Keun-Hyeung</au><au>Chi, Seung-Wook</au><au>Hong, Seong-Yu</au><au>Choi, Byoung-Wook</au><au>Moon, Hong-Mo</au><au>Choi, Byong-Seok</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unusually stable helical kink in the antimicrobial peptide — A derivative of gaegurin</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1996-09-02</date><risdate>1996</risdate><volume>392</volume><issue>3</issue><spage>309</spage><epage>312</epage><pages>309-312</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The structure of an active analog of the antibacterial peptide gaegurin was investigated by CD and NMR spectroscopy. The NOE connectivities showed that 21 out of 24 residues formed an α-helix despite the presence of a central proline. CD and NMR analysis indicates that the helix is in fast equilibrium with random coil. From chemical shift analysis of the amide protons, the distances of hydrogen bonding in the helix were calculated, and manifested obvious periodicity which implied a kink in the middle of the helix. 1D amide proton exchange experiments provided further evidence of an exceptionally stable kink. It is inferred that this kink is important not only to the function of the peptide but also to the early stage of the folding as a nucleation site.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>8774869</pmid><doi>10.1016/0014-5793(96)00840-X</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1996-09, Vol.392 (3), p.309-312 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; Alma/SFX Local Collection |
| subjects | 9-fluorenylmethyloxycarbonyl Anti-Infective Agents - chemistry Circular Dichroism Fmoc Gaegurin Hydrogen Bonding Kink Magnetic Resonance Spectroscopy Models, Molecular NMR NOE NOESY nuclear Overhauser enhancement nuclear Overhauser enhancement spectroscopy one-dimensional Peptides - chemistry Peptides - pharmacology Protein Conformation reverse phase-high performance liquid chromatography RP-HPLC Structure-Activity Relationship TOCSY total correlation spectroscopy α-Helix |
| title | Unusually stable helical kink in the antimicrobial peptide — A derivative of gaegurin |
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