MersV1, Main, Exploration, bibRecord, 003335

Cyclic and hairpin peptide complexes of heme.

Identifieur interne : 003335 ( Main/Exploration ); précédent : 003334; suivant : 003336

Cyclic and hairpin peptide complexes of heme.

Auteurs : Michael M. Rosenblatt [États-Unis] ; David L. Huffman ; Xiaotang Wang ; Henriette A. Remmer ; Kenneth S. Suslick

Source :

Journal of the American Chemical Society [ 0002-7863 ] ; 2002.

RBID : pubmed:12381164

Descripteurs français

KwdFr :
- Cinétique, Conformation des protéines, Disulfures (), Hème (), Modèles moléculaires, Peptides cycliques (), Résonance magnétique nucléaire biomoléculaire.
MESH :
- Cinétique, Conformation des protéines, Disulfures, Hème, Modèles moléculaires, Peptides cycliques, Résonance magnétique nucléaire biomoléculaire.

English descriptors

KwdEn :
- Disulfides (chemistry), Heme (chemistry), Kinetics, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Peptides, Cyclic (chemistry), Protein Conformation.
MESH :
- chemical , chemistry : Disulfides, Heme, Peptides, Cyclic.
- Kinetics, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation.

Abstract

We have synthesized and characterized a new class of heme-peptide complexes using disulfide-linked hairpin-turn and cyclic peptides and compared these to their linear analogues. The binding affinities, helicities, and mechanism of binding of linear, hairpin, and cyclic peptides to [FeIII(coproporphyrin-I)]+ have been determined. In a minimalist approach, we utilize amphiphilic peptide sequences (15-mers), where a central histidine provides heme ligation, and the hydrophobic effect is used to optimize heme-peptide complex stability. We have incorporated disulfide bridges between amphiphilic peptides to make hairpin and even cyclic peptides that bind heme extremely well, roughly 5 x 106 times more strongly than histidine itself. CD studies show that the cyclic peptide heme complexes are completely alpha-helical. NMR spectra of paramagnetic complexes of the peptides show that the 15-mer peptides bind sequentially, with an observable monopeptide, high-spin intermediate. In contrast, the cyclic peptide complexes ligate both imidazoles cooperatively to the heme, producing only a low-spin complex. Electrochemical measurements of the E1/2 of the FeIII(coproporphyrin-I)+ complexes of these peptides are all at fairly low potentials, ranging from -215 to -252 mV versus NHE at pH 7.

DOI: 10.1021/ja020912w
PubMed: 12381164

Affiliations:

États-Unis

Le document en format XML

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<term>Peptides, Cyclic (chemistry)</term>
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<term>Conformation des protéines</term>
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<term>Hème ()</term>
<term>Modèles moléculaires</term>
<term>Peptides cycliques ()</term>
<term>Résonance magnétique nucléaire biomoléculaire</term>
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<front><div type="abstract" xml:lang="en">We have synthesized and characterized a new class of heme-peptide complexes using disulfide-linked hairpin-turn and cyclic peptides and compared these to their linear analogues. The binding affinities, helicities, and mechanism of binding of linear, hairpin, and cyclic peptides to [FeIII(coproporphyrin-I)]+ have been determined. In a minimalist approach, we utilize amphiphilic peptide sequences (15-mers), where a central histidine provides heme ligation, and the hydrophobic effect is used to optimize heme-peptide complex stability. We have incorporated disulfide bridges between amphiphilic peptides to make hairpin and even cyclic peptides that bind heme extremely well, roughly 5 x 106 times more strongly than histidine itself. CD studies show that the cyclic peptide heme complexes are completely alpha-helical. NMR spectra of paramagnetic complexes of the peptides show that the 15-mer peptides bind sequentially, with an observable monopeptide, high-spin intermediate. In contrast, the cyclic peptide complexes ligate both imidazoles cooperatively to the heme, producing only a low-spin complex. Electrochemical measurements of the E1/2 of the FeIII(coproporphyrin-I)+ complexes of these peptides are all at fairly low potentials, ranging from -215 to -252 mV versus NHE at pH 7.</div>
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Serveur d'exploration MERS

Cyclic and hairpin peptide complexes of heme.

Cyclic and hairpin peptide complexes of heme.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

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