ArticleInorganic chemistry2008
Design of thiolate rich metal binding sites within a peptidic framework.
Article in Inorganic chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 49 citations in OpenAlex.
- Photocatalytic Hydrogen Evolution by a De Novo Designed Metalloprotein that Undergoes Ni-Mediated Oligomerization Shift.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- An Extremely Stable Interprotein Tetrahedral Hg(Cys)Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Chemical-Shift Standards forInorganic chemistry · 2022Article
- Efficient Removal of Hg(II) from Water under Mildly Acidic Conditions with Hierarchical SiOMaterials (Basel, Switzerland) · 2022Article
- A De Novo-Designed Artificial Metallopeptide Hydrogenase: Insights into Photochemical Processes and the Role of Protonated Cys.ChemSusChem · 2021Article
- Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Formation of Hg(II) Tetrathiolate Complexes with Cysteine at Neutral pH.Canadian journal of chemistry · 2016Article
- Methods for Solving Highly Symmetric De Novo Designed Metalloproteins: Crystallographic Examination of a Novel Three-Stranded Coiled-Coil Structure Containing d-Amino Acids.Methods in enzymology · 2016Article
- Sculpting Metal-binding Environments inIsrael journal of chemistry · 2015Article
- Designing hydrolytic zinc metalloenzymes.Biochemistry · 2014Review
- Designing functional metalloproteins: from structural to catalytic metal sites.Coordination chemistry reviews · 2013Article
- Probing the coordination environment of the human copper chaperone HAH1: characterization of Hg(II)-bridged homodimeric species in solution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2013Article
- Design of a three-helix bundle capable of binding heavy metals in a triscysteine environment.Angewandte Chemie (International ed. in English) · 2011Article
- Controlling and fine tuning the physical properties of two identical metal coordination sites in de novo designed three stranded coiled coil peptides.Journal of the American Chemical Society · 2011Article
- Structural comparisons of apo- and metalated three-stranded coiled coils clarify metal binding determinants in thiolate containing designed peptides.Journal of the American Chemical Society · 2010Article
- Cadmium(II) complex formation with glutathione.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
- Cadmium(II) complex formation with cysteine and penicillamine.Inorganic chemistry · 2009Article
- Harnessing natures ability to control metal ion coordination geometry using de novo designed peptides.Dalton transactions (Cambridge, England : 2003) · 2009Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
A de novo protein design strategy provides a powerful tool to elucidate how heavy metals interact with proteins.Cysteine derivatives of the TRI peptide family (Ac-G(LKALEEK)4G-NH2) have been shown to bind heavy metals in an unusual trigonal geometry. Our present objective was to design binding sites in R-helical scaffolds that are able to form higher coordination number complexes with Cd(II) and Hg(II). Herein, we evaluate the binding of Cd(II) and Hg(II) to double cysteine substituted TRI peptides lacking intervening leucines between sulfurs in the heptads. We compare a -Cysd-X-X-X-Cysa- binding motif found in TRIL12CL16C to the more common -Cysa-X-X-Cysd- sequence of native proteins found in TRIL9CL12C. Compared to TRI, these substitutions destabilize the helical aggregates,leading to mixtures of two- and three-stranded bundles. The three-stranded coiled coils are stabilized by the addition of metals. TRIL9CL12C forms distorted tetrahedral complexes with both Cd(II) and Hg(II), as supported by UV-vis,CD, 113Cd NMR, 199Hg NMR and 111mCd PAC spectroscopy. Additionally, these signatures are very similar to those found for heavy metal substituted rubredoxin. These results suggest that in terms of Hg(II) binding, TRIL9CL12Ccan be considered as a good mimic of the metallochaperone HAH1, that has previously been shown to form protein dimers. TRIL12CL16C has limited ability to generate homoleptic tetrahedral complexes (Cd(SR)42-). These type of complexes were identified only for Hg(II). However, the spectroscopic signatures suggest a different geometry around the metal ion, demonstrating that effective metal sequestration into the hydrophobic interior of the bundle requires more than simply adding two sulfur residues in adjacent layers of the peptide core. Thus, proper design of metal binding sites must also consider the orientation of cysteine sidechains in a vs d positions of the heptads.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.