Site-specific modification of α-helical peptides with electron donors and acceptors

Bassil I. Dahiyat; Thomas J. Meade; Stephen L. Mayo

doi:10.1016/0020-1693(95)04909-6

Site-specific modification of α-helical peptides with electron donors and acceptors

Bassil I. Dahiyat, Thomas J. Meade^*, Stephen L. Mayo

^*Corresponding author for this work

Chemistry

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

15 Scopus citations

Abstract

We have prepared a histidine containing monomeric α-helical peptide, ETH6 (A₂KA₄KA₂HA₆HA₄KA ₄K) in order to study long-range electron transfer (ET). This peptide was site-specifically labeled with a ruthenium (donor) at one histidine and a second ruthenium (acceptor) at a second histidine located on the same peptide. Both the unlabeled peptide and the singly labeled peptide-metal complex, Ru(bpy)₂(im)(His)-ETH6, were shown to form stable monomeric α-helical structures as determined by circular dichroism. Ru(NH₃)₄(py) was coupled to Ru(bpy)₂(im)(His)-ETH6, forming a Ru(bpy)₂(im)(His)-ETH6-(His)Ru(NH₃)4(py) donor-acceptor complex. The synthesis and characterization of these peptides provide an entry into a series of molecules that are ideally suited to evaluate pathway differences such as H-bond mediated versus backbone-coupled long-range ET in protein α-helices.

Original language	English (US)
Pages (from-to)	207-212
Number of pages	6
Journal	Inorganica Chimica Acta
Volume	243
Issue number	1-2
DOIs	https://doi.org/10.1016/0020-1693(95)04909-6
State	Published - Feb 29 1996

Keywords

Electron transfer
Ruthenium complexes
α-Helical peptides complexes

ASJC Scopus subject areas

Physical and Theoretical Chemistry
Inorganic Chemistry
Materials Chemistry

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10.1016/0020-1693(95)04909-6

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title = "Site-specific modification of α-helical peptides with electron donors and acceptors",

abstract = "We have prepared a histidine containing monomeric α-helical peptide, ETH6 (A2KA4KA2HA6HA4KA 4K) in order to study long-range electron transfer (ET). This peptide was site-specifically labeled with a ruthenium (donor) at one histidine and a second ruthenium (acceptor) at a second histidine located on the same peptide. Both the unlabeled peptide and the singly labeled peptide-metal complex, Ru(bpy)2(im)(His)-ETH6, were shown to form stable monomeric α-helical structures as determined by circular dichroism. Ru(NH3)4(py) was coupled to Ru(bpy)2(im)(His)-ETH6, forming a Ru(bpy)2(im)(His)-ETH6-(His)Ru(NH3)4(py) donor-acceptor complex. The synthesis and characterization of these peptides provide an entry into a series of molecules that are ideally suited to evaluate pathway differences such as H-bond mediated versus backbone-coupled long-range ET in protein α-helices.",

keywords = "Electron transfer, Ruthenium complexes, α-Helical peptides complexes",

author = "Dahiyat, {Bassil I.} and Meade, {Thomas J.} and Mayo, {Stephen L.}",

note = "Funding Information: dation, the David and Lucile Packard Foundation and the Searle Scholars Program. B.I.D. is partially supported by NIH Training Grant GM 08346. T.J.M. acknowledges support from the Petroleum Research Fund, American Chemical Society and the Research Corporation. Funding Information: We thank H. Qian for the computer program implementing Lifson-Roig theory, G. Hathaway for mass spectral analysis and J.F. Kayyem for helpful discussions. S.L.M. acknowledges support from the Rita Allen Foun-",

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doi = "10.1016/0020-1693(95)04909-6",

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T1 - Site-specific modification of α-helical peptides with electron donors and acceptors

AU - Dahiyat, Bassil I.

AU - Meade, Thomas J.

AU - Mayo, Stephen L.

N1 - Funding Information: dation, the David and Lucile Packard Foundation and the Searle Scholars Program. B.I.D. is partially supported by NIH Training Grant GM 08346. T.J.M. acknowledges support from the Petroleum Research Fund, American Chemical Society and the Research Corporation. Funding Information: We thank H. Qian for the computer program implementing Lifson-Roig theory, G. Hathaway for mass spectral analysis and J.F. Kayyem for helpful discussions. S.L.M. acknowledges support from the Rita Allen Foun-

PY - 1996/2/29

Y1 - 1996/2/29

N2 - We have prepared a histidine containing monomeric α-helical peptide, ETH6 (A2KA4KA2HA6HA4KA 4K) in order to study long-range electron transfer (ET). This peptide was site-specifically labeled with a ruthenium (donor) at one histidine and a second ruthenium (acceptor) at a second histidine located on the same peptide. Both the unlabeled peptide and the singly labeled peptide-metal complex, Ru(bpy)2(im)(His)-ETH6, were shown to form stable monomeric α-helical structures as determined by circular dichroism. Ru(NH3)4(py) was coupled to Ru(bpy)2(im)(His)-ETH6, forming a Ru(bpy)2(im)(His)-ETH6-(His)Ru(NH3)4(py) donor-acceptor complex. The synthesis and characterization of these peptides provide an entry into a series of molecules that are ideally suited to evaluate pathway differences such as H-bond mediated versus backbone-coupled long-range ET in protein α-helices.

AB - We have prepared a histidine containing monomeric α-helical peptide, ETH6 (A2KA4KA2HA6HA4KA 4K) in order to study long-range electron transfer (ET). This peptide was site-specifically labeled with a ruthenium (donor) at one histidine and a second ruthenium (acceptor) at a second histidine located on the same peptide. Both the unlabeled peptide and the singly labeled peptide-metal complex, Ru(bpy)2(im)(His)-ETH6, were shown to form stable monomeric α-helical structures as determined by circular dichroism. Ru(NH3)4(py) was coupled to Ru(bpy)2(im)(His)-ETH6, forming a Ru(bpy)2(im)(His)-ETH6-(His)Ru(NH3)4(py) donor-acceptor complex. The synthesis and characterization of these peptides provide an entry into a series of molecules that are ideally suited to evaluate pathway differences such as H-bond mediated versus backbone-coupled long-range ET in protein α-helices.

KW - Electron transfer

KW - Ruthenium complexes

KW - α-Helical peptides complexes

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SN - 0020-1693

IS - 1-2

ER -

Site-specific modification of α-helical peptides with electron donors and acceptors

Abstract

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