Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA

Lauren A. Levine; Christopher M. Morgan; Kristi Ohr; Mary Elizabeth Williams

doi:10.1021/ja055162f

Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA

Lauren A. Levine, Christopher M. Morgan, Kristi Ohr, Mary Elizabeth Williams

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

This paper reports the binding of an artificial tetrapeptide to which are tethered four Pt(II) complexes (i.e., [Pt(tpy)(py)]₄⁸⁺) with a 12 base pair duplex DNA oligonucleotide. Isothermal Titration Calorimetry reveals that two tetrametallic peptides stoichiometrically bind to each DNA duplex with a binding constant, K_B, of 1.7 × 10⁶ M^-1, with a change in free energy of -8.5 kcal/mol. This KB represents an affinity 2 orders of magnitude greater than that of the monometallic analogue [Pt(tpy)(pic)]²⁺ for the same dsDNA sequence. The metalated peptides bind by intercalation into the DNA, partially unwinding the helix while stabilizing the structure, causing an increase in the dsDNA melting temperature of 25 °C.

Original language	English (US)
Pages (from-to)	16764-16765
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	48
DOIs	https://doi.org/10.1021/ja055162f
State	Published - Dec 7 2005

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja055162f

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title = "Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA",

abstract = "This paper reports the binding of an artificial tetrapeptide to which are tethered four Pt(II) complexes (i.e., [Pt(tpy)(py)]48+) with a 12 base pair duplex DNA oligonucleotide. Isothermal Titration Calorimetry reveals that two tetrametallic peptides stoichiometrically bind to each DNA duplex with a binding constant, KB, of 1.7 × 106 M-1, with a change in free energy of -8.5 kcal/mol. This KB represents an affinity 2 orders of magnitude greater than that of the monometallic analogue [Pt(tpy)(pic)]2+ for the same dsDNA sequence. The metalated peptides bind by intercalation into the DNA, partially unwinding the helix while stabilizing the structure, causing an increase in the dsDNA melting temperature of 25 °C.",

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T1 - Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA

AU - Levine, Lauren A.

AU - Morgan, Christopher M.

AU - Ohr, Kristi

AU - Williams, Mary Elizabeth

PY - 2005/12/7

Y1 - 2005/12/7

N2 - This paper reports the binding of an artificial tetrapeptide to which are tethered four Pt(II) complexes (i.e., [Pt(tpy)(py)]48+) with a 12 base pair duplex DNA oligonucleotide. Isothermal Titration Calorimetry reveals that two tetrametallic peptides stoichiometrically bind to each DNA duplex with a binding constant, KB, of 1.7 × 106 M-1, with a change in free energy of -8.5 kcal/mol. This KB represents an affinity 2 orders of magnitude greater than that of the monometallic analogue [Pt(tpy)(pic)]2+ for the same dsDNA sequence. The metalated peptides bind by intercalation into the DNA, partially unwinding the helix while stabilizing the structure, causing an increase in the dsDNA melting temperature of 25 °C.

AB - This paper reports the binding of an artificial tetrapeptide to which are tethered four Pt(II) complexes (i.e., [Pt(tpy)(py)]48+) with a 12 base pair duplex DNA oligonucleotide. Isothermal Titration Calorimetry reveals that two tetrametallic peptides stoichiometrically bind to each DNA duplex with a binding constant, KB, of 1.7 × 106 M-1, with a change in free energy of -8.5 kcal/mol. This KB represents an affinity 2 orders of magnitude greater than that of the monometallic analogue [Pt(tpy)(pic)]2+ for the same dsDNA sequence. The metalated peptides bind by intercalation into the DNA, partially unwinding the helix while stabilizing the structure, causing an increase in the dsDNA melting temperature of 25 °C.

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Tetraplatinated artificial oligopeptides afford high affinity intercalation into dsDNA

Abstract

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