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

14 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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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.}",

year = "1996",

month = feb,

day = "29",

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

language = "English (US)",

volume = "243",

pages = "207--212",

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AU - Dahiyat, Bassil I.

AU - Meade, Thomas J.

AU - Mayo, Stephen L.

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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