Antimicrobial lipopeptaibol trichogin GA IV: role of the three Aib residues on conformation and bioactivity
The lipopeptaibol trichogin GA IV is a natural, non-ribosomally synthesized, antimicrobial peptide remarkably resistant to the action of hydrolytic enzymes. This feature may be connected to the multiple presence in its sequence of the non-coded residue α-aminoisobutyric acid (Aib), which is known to...
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| Veröffentlicht in: | Amino acids 2012-10, Vol.43 (4), p.1761-1777 |
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| creator | De Zotti, Marta Biondi, Barbara Park, Yoonkyung Hahm, Kyung-Soo Crisma, Marco Toniolo, Claudio Formaggio, Fernando |
| description | The lipopeptaibol trichogin GA IV is a natural, non-ribosomally synthesized, antimicrobial peptide remarkably resistant to the action of hydrolytic enzymes. This feature may be connected to the multiple presence in its sequence of the non-coded residue α-aminoisobutyric acid (Aib), which is known to be responsible for the adoption of particularly stable helical structures already at the level of short peptides. To investigate the role of Aib residues on the 3D-structure and bioactivity of trichogin GA IV, we synthesized and fully characterized four analogs where one or two Aib residues are replaced by
l
-Leu. Our extensive conformational studies (including an X-ray diffraction analysis) and biological assays performed on these analogs showed that the Aib to
l
-Leu replacements do not affect the resistance to proteolysis, but modulate the bioactivity of trichogin GA IV in a 3D-structure related manner. |
| doi_str_mv | 10.1007/s00726-012-1261-7 |
| format | Article |
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l
-Leu. Our extensive conformational studies (including an X-ray diffraction analysis) and biological assays performed on these analogs showed that the Aib to
l
-Leu replacements do not affect the resistance to proteolysis, but modulate the bioactivity of trichogin GA IV in a 3D-structure related manner.</description><identifier>ISSN: 0939-4451</identifier><identifier>EISSN: 1438-2199</identifier><identifier>DOI: 10.1007/s00726-012-1261-7</identifier><identifier>PMID: 22484376</identifier><language>eng</language><publisher>Vienna: Springer Vienna</publisher><subject><![CDATA[Amino Acid Substitution ; Aminoisobutyric Acids - chemistry ; Analytical Chemistry ; Anti-Infective Agents - chemical synthesis ; Anti-Infective Agents - pharmacology ; Biochemical Engineering ; Biochemistry ; Biomedical and Life Sciences ; Candida albicans - drug effects ; Candida albicans - growth & development ; Circular Dichroism ; Escherichia coli - drug effects ; Escherichia coli - growth & development ; Kinetics ; Leucine - chemistry ; Life Sciences ; Lipopeptides - chemical synthesis ; Lipopeptides - pharmacology ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Neurobiology ; Original Article ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteomics ; Pseudomonas aeruginosa - drug effects ; Pseudomonas aeruginosa - growth & development ; Spectroscopy, Fourier Transform Infrared ; Staphylococcus aureus - drug effects ; Staphylococcus aureus - growth & development ; Staphylococcus epidermidis - drug effects ; Staphylococcus epidermidis - growth & development ; Structure-Activity Relationship ; Thermodynamics ; Trichosporon - drug effects ; Trichosporon - growth & development ; X-Ray Diffraction]]></subject><ispartof>Amino acids, 2012-10, Vol.43 (4), p.1761-1777</ispartof><rights>Springer-Verlag 2012</rights><rights>Springer-Verlag Wien 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c471t-8090ceda9143295a944a7833ef134eafbc79db40a3b5604f8cb42901c4d0a03</citedby><cites>FETCH-LOGICAL-c471t-8090ceda9143295a944a7833ef134eafbc79db40a3b5604f8cb42901c4d0a03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00726-012-1261-7$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00726-012-1261-7$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22484376$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>De Zotti, Marta</creatorcontrib><creatorcontrib>Biondi, Barbara</creatorcontrib><creatorcontrib>Park, Yoonkyung</creatorcontrib><creatorcontrib>Hahm, Kyung-Soo</creatorcontrib><creatorcontrib>Crisma, Marco</creatorcontrib><creatorcontrib>Toniolo, Claudio</creatorcontrib><creatorcontrib>Formaggio, Fernando</creatorcontrib><title>Antimicrobial lipopeptaibol trichogin GA IV: role of the three Aib residues on conformation and bioactivity</title><title>Amino acids</title><addtitle>Amino Acids</addtitle><addtitle>Amino Acids</addtitle><description>The lipopeptaibol trichogin GA IV is a natural, non-ribosomally synthesized, antimicrobial peptide remarkably resistant to the action of hydrolytic enzymes. This feature may be connected to the multiple presence in its sequence of the non-coded residue α-aminoisobutyric acid (Aib), which is known to be responsible for the adoption of particularly stable helical structures already at the level of short peptides. To investigate the role of Aib residues on the 3D-structure and bioactivity of trichogin GA IV, we synthesized and fully characterized four analogs where one or two Aib residues are replaced by
l
-Leu. Our extensive conformational studies (including an X-ray diffraction analysis) and biological assays performed on these analogs showed that the Aib to
l
-Leu replacements do not affect the resistance to proteolysis, but modulate the bioactivity of trichogin GA IV in a 3D-structure related manner.</description><subject>Amino Acid Substitution</subject><subject>Aminoisobutyric Acids - chemistry</subject><subject>Analytical Chemistry</subject><subject>Anti-Infective Agents - chemical synthesis</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Biochemical Engineering</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Candida albicans - drug effects</subject><subject>Candida albicans - growth & development</subject><subject>Circular Dichroism</subject><subject>Escherichia coli - drug effects</subject><subject>Escherichia coli - growth & development</subject><subject>Kinetics</subject><subject>Leucine - chemistry</subject><subject>Life Sciences</subject><subject>Lipopeptides - chemical synthesis</subject><subject>Lipopeptides - pharmacology</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Neurobiology</subject><subject>Original Article</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Proteomics</subject><subject>Pseudomonas aeruginosa - drug effects</subject><subject>Pseudomonas aeruginosa - growth & development</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Staphylococcus aureus - growth & development</subject><subject>Staphylococcus epidermidis - drug effects</subject><subject>Staphylococcus epidermidis - growth & development</subject><subject>Structure-Activity Relationship</subject><subject>Thermodynamics</subject><subject>Trichosporon - drug effects</subject><subject>Trichosporon - growth & development</subject><subject>X-Ray Diffraction</subject><issn>0939-4451</issn><issn>1438-2199</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkU1PHSEUhkmjqbe2P6CbhsRNN6McYGBwd3PTWhMTF5puCTCMojPDFLgm_nsx1zamiXHBIYTnvOfjRegrkGMgRJ7kGqhoCNAGqIBGfkAr4KxrKCi1h1ZEMdVw3sIB-pTzHalgB-IjOqCUd5xJsUL367mEKbgUbTAjHsMSF78UE2wccUnB3cabMOOzNT7_fYpTHD2OAy63vp7kPV4Hi5PPod_6jOOMXZyHmCZTQn2Yucc2RONKeAjl8TPaH8yY_ZeX-xBd_fxxvfnVXFyenW_WF43jEkrTEUWc742qo1DVGsW5kR1jfgDGvRmsk6q3nBhmW0H40DnLqSLgeE8MYYfo-051SfFP7aroKWTnx9HMPm6zBmCCt5KBeB8lQlEihOQVPfoPvYvbNNcxNNTmFIOOtpWCHVX3mXPyg15SmEx6rFL62TK9s0xXJ_SzZVrWnG8vyls7-f5fxl-PKkB3QK5f841Pr0q_qfoESLSgYg</recordid><startdate>20121001</startdate><enddate>20121001</enddate><creator>De Zotti, Marta</creator><creator>Biondi, Barbara</creator><creator>Park, Yoonkyung</creator><creator>Hahm, Kyung-Soo</creator><creator>Crisma, Marco</creator><creator>Toniolo, Claudio</creator><creator>Formaggio, Fernando</creator><general>Springer Vienna</general><general>Springer Nature B.V</general><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>3V.</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20121001</creationdate><title>Antimicrobial lipopeptaibol trichogin GA IV: role of the three Aib residues on conformation and bioactivity</title><author>De Zotti, Marta ; Biondi, Barbara ; Park, Yoonkyung ; Hahm, Kyung-Soo ; Crisma, Marco ; Toniolo, Claudio ; Formaggio, Fernando</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c471t-8090ceda9143295a944a7833ef134eafbc79db40a3b5604f8cb42901c4d0a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Substitution</topic><topic>Aminoisobutyric Acids - chemistry</topic><topic>Analytical Chemistry</topic><topic>Anti-Infective Agents - chemical synthesis</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>Biochemical Engineering</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Candida albicans - drug effects</topic><topic>Candida albicans - growth & development</topic><topic>Circular Dichroism</topic><topic>Escherichia coli - drug effects</topic><topic>Escherichia coli - growth & development</topic><topic>Kinetics</topic><topic>Leucine - chemistry</topic><topic>Life Sciences</topic><topic>Lipopeptides - chemical synthesis</topic><topic>Lipopeptides - pharmacology</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Neurobiology</topic><topic>Original Article</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Proteomics</topic><topic>Pseudomonas aeruginosa - drug effects</topic><topic>Pseudomonas aeruginosa - growth & development</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Staphylococcus aureus - growth & development</topic><topic>Staphylococcus epidermidis - drug effects</topic><topic>Staphylococcus epidermidis - growth & development</topic><topic>Structure-Activity Relationship</topic><topic>Thermodynamics</topic><topic>Trichosporon - drug effects</topic><topic>Trichosporon - growth & development</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>De Zotti, Marta</creatorcontrib><creatorcontrib>Biondi, Barbara</creatorcontrib><creatorcontrib>Park, Yoonkyung</creatorcontrib><creatorcontrib>Hahm, Kyung-Soo</creatorcontrib><creatorcontrib>Crisma, Marco</creatorcontrib><creatorcontrib>Toniolo, Claudio</creatorcontrib><creatorcontrib>Formaggio, Fernando</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Amino acids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>De Zotti, Marta</au><au>Biondi, Barbara</au><au>Park, Yoonkyung</au><au>Hahm, Kyung-Soo</au><au>Crisma, Marco</au><au>Toniolo, Claudio</au><au>Formaggio, Fernando</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antimicrobial lipopeptaibol trichogin GA IV: role of the three Aib residues on conformation and bioactivity</atitle><jtitle>Amino acids</jtitle><stitle>Amino Acids</stitle><addtitle>Amino Acids</addtitle><date>2012-10-01</date><risdate>2012</risdate><volume>43</volume><issue>4</issue><spage>1761</spage><epage>1777</epage><pages>1761-1777</pages><issn>0939-4451</issn><eissn>1438-2199</eissn><abstract>The lipopeptaibol trichogin GA IV is a natural, non-ribosomally synthesized, antimicrobial peptide remarkably resistant to the action of hydrolytic enzymes. This feature may be connected to the multiple presence in its sequence of the non-coded residue α-aminoisobutyric acid (Aib), which is known to be responsible for the adoption of particularly stable helical structures already at the level of short peptides. To investigate the role of Aib residues on the 3D-structure and bioactivity of trichogin GA IV, we synthesized and fully characterized four analogs where one or two Aib residues are replaced by
l
-Leu. Our extensive conformational studies (including an X-ray diffraction analysis) and biological assays performed on these analogs showed that the Aib to
l
-Leu replacements do not affect the resistance to proteolysis, but modulate the bioactivity of trichogin GA IV in a 3D-structure related manner.</abstract><cop>Vienna</cop><pub>Springer Vienna</pub><pmid>22484376</pmid><doi>10.1007/s00726-012-1261-7</doi><tpages>17</tpages></addata></record> |
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| subjects | Amino Acid Substitution Aminoisobutyric Acids - chemistry Analytical Chemistry Anti-Infective Agents - chemical synthesis Anti-Infective Agents - pharmacology Biochemical Engineering Biochemistry Biomedical and Life Sciences Candida albicans - drug effects Candida albicans - growth & development Circular Dichroism Escherichia coli - drug effects Escherichia coli - growth & development Kinetics Leucine - chemistry Life Sciences Lipopeptides - chemical synthesis Lipopeptides - pharmacology Magnetic Resonance Spectroscopy Models, Molecular Neurobiology Original Article Protein Structure, Secondary Protein Structure, Tertiary Proteomics Pseudomonas aeruginosa - drug effects Pseudomonas aeruginosa - growth & development Spectroscopy, Fourier Transform Infrared Staphylococcus aureus - drug effects Staphylococcus aureus - growth & development Staphylococcus epidermidis - drug effects Staphylococcus epidermidis - growth & development Structure-Activity Relationship Thermodynamics Trichosporon - drug effects Trichosporon - growth & development X-Ray Diffraction |
| title | Antimicrobial lipopeptaibol trichogin GA IV: role of the three Aib residues on conformation and bioactivity |
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