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An azacrown-functionalized peptide as a metal ion based catalyst for the cleavage of a RNA-model substrate

2000; Wiley; Volume: 55; Issue: 6 Linguagem: Inglês

10.1002/1097-0282(2000)55

1097-0282

Paola Rossi, Fulvia Felluga, Paolo Tecilla, Fernando Formaggio, Marco Crisma, Claudio Toniolo, Paolo Scrimin,

DNA and Nucleic Acid Chemistry

Peptide ScienceVolume 55, Issue 6 p. 496-501 An azacrown-functionalized peptide as a metal ion based catalyst for the cleavage of a RNA-model substrate Paola Rossi, Paola Rossi University of Trieste, Department of Chemical Sciences, via L. Giorgieri, 1 34127 Trieste, ItalySearch for more papers by this authorFulvia Felluga, Fulvia Felluga University of Trieste, Department of Chemical Sciences, via L. Giorgieri, 1 34127 Trieste, ItalySearch for more papers by this authorPaolo Tecilla, Paolo Tecilla University of Trieste, Department of Chemical Sciences, via L. Giorgieri, 1 34127 Trieste, ItalySearch for more papers by this authorFernando Formaggio, Fernando Formaggio University of Padova, Department of Organic Chemistry and CNR Center CSB, via L. Marzolo, 1 35131 Padova, ItalySearch for more papers by this authorMarco Crisma, Marco Crisma University of Padova, Department of Organic Chemistry and CNR Center CSB, via L. Marzolo, 1 35131 Padova, ItalySearch for more papers by this authorClaudio Toniolo, Claudio Toniolo University of Padova, Department of Organic Chemistry and CNR Center CSB, via L. Marzolo, 1 35131 Padova, ItalySearch for more papers by this authorPaolo Scrimin, Corresponding Author Paolo Scrimin scrimin@mail.chor.unipd.it University of Padova, Department of Organic Chemistry and CNR Center CMRO, via L. Marzolo, 1 35131 Padova, ItalyUniversity of Padova, Department of Organic Chemistry and CNR Center CMRO, via L. Marzolo, 1 35131 Padova, Italy===Search for more papers by this author Paola Rossi, Paola Rossi University of Trieste, Department of Chemical Sciences, via L. Giorgieri, 1 34127 Trieste, ItalySearch for more papers by this authorFulvia Felluga, Fulvia Felluga University of Trieste, Department of Chemical Sciences, via L. Giorgieri, 1 34127 Trieste, ItalySearch for more papers by this authorPaolo Tecilla, Paolo Tecilla University of Trieste, Department of Chemical Sciences, via L. Giorgieri, 1 34127 Trieste, ItalySearch for more papers by this authorFernando Formaggio, Fernando Formaggio University of Padova, Department of Organic Chemistry and CNR Center CSB, via L. Marzolo, 1 35131 Padova, ItalySearch for more papers by this authorMarco Crisma, Marco Crisma University of Padova, Department of Organic Chemistry and CNR Center CSB, via L. Marzolo, 1 35131 Padova, ItalySearch for more papers by this authorClaudio Toniolo, Claudio Toniolo University of Padova, Department of Organic Chemistry and CNR Center CSB, via L. Marzolo, 1 35131 Padova, ItalySearch for more papers by this authorPaolo Scrimin, Corresponding Author Paolo Scrimin scrimin@mail.chor.unipd.it University of Padova, Department of Organic Chemistry and CNR Center CMRO, via L. Marzolo, 1 35131 Padova, ItalyUniversity of Padova, Department of Organic Chemistry and CNR Center CMRO, via L. Marzolo, 1 35131 Padova, Italy===Search for more papers by this author First published: 12 January 2004 https://doi.org/10.1002/1097-0282(2000)55:6 3.0.CO;2-6Citations: 36Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Abstract The previously synthesized, terminally blocked heptapeptide Ac–Aib–ATANP–Aib–Aib–ATANP–Aib–Aib–OMe (1a), where ATANP is (S)-2-amino-3-[1-(1,4,7-triazacyclononane)]propanoic acid and Aib is α-aminoisobutyric acid, which is soluble in neutral water where it largely adopts a 310-helical conformation, has been studied, as bimetallic complex [metal ions: Cu(II), Ni(II), Zn(II)], for the transphosphorylation catalysis of the RNA-model substrate 2-(hydroxypropyl)-p-nitrophenyl phosphate (HPNP). A detailed analysis was carried out with the Zn(II) dinuclear complex. Comparison with the mononuclear Zn(II) complex with 1,4,7-triazacyclononane (3) points to cooperativity between the two Zn(II) ions in the process catalyzed by 1a–2Zn(II). On the contrary, the dinuclear Zn(II) complex of dipeptide Ac–(ATANP)2–OMe (2), lacking any ordered conformation, is less active than 3-Zn(II). The kinetic analysis suggests the following: (a) the peptide is conformationally very robust and does not loose activity up to 50°C; (b) the substrate binds to the peptide–Zn(II) complex, although not all modes of complexation allow us to take advantage of the cooperativity between the two metal centers. The maximum rate acceleration estimated at pH 7 for the fully bound substrate is ca. 200-fold compared with the uncatalyzed process. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 55: 496–501, 2000 Citing Literature Volume55, Issue62000Pages 496-501 RelatedInformation