A novel spin-labeled amino acid derivative for use in peptide synthesis: (9-fluorenylmethyloxycarbonyl)-2,2,6,6-tetramethylpiperidine-N-oxyl-4-amino-4-carboxylic acid

Marchetto, Reinaldo; Schreier, Shirley; Nakaie, Clóvis R.

doi:10.1021/ja00076a093

Cited by 151 publications

(136 citation statements)

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“…In addition, we were also able to discriminate differences between ligand specificities for ACE or AT 1 by using the TOAC 3 -Ang II derivative, where TOAC (2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid) is a spin-labeled amino acid that was internally coupled to Ang II. 21 TOAC 3 -Ang II, which is not able to bind or activate AT 1 receptors, 11,14 could stimulate CHO-ACE cells, increasing intracellular Ca 2ϩ , again suggesting a specific calcium signaling by ACE. In addition, we could demonstrate that the effect was specific for Ang II, because other peptides related to ACE metabolism, such as BK, BK1-5, Ac-SDKP, and Ang 1-7, were inactive.…”

Section: Discussionmentioning

confidence: 96%

Angiotensin II Binding to Angiotensin I–Converting Enzyme Triggers Calcium Signaling

et al. 2011

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Section: Discussionmentioning

confidence: 96%

Angiotensin II Binding to Angiotensin I–Converting Enzyme Triggers Calcium Signaling

et al. 2011

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“…The former strategy is usually applied in solid-state [26] or solution-state [27] synthesis of peptides and for oligonucleotides [15] and allows a broad variation of labeling chemistry [28]. In this scenario, one often aims for a rigid coupling of the label to the backbone of the macromolecule and for the least possible conformational ambiguity of the label.…”

Section: Labeling Strategy and Common Spin Labelsmentioning

confidence: 99%

“…For peptides, this can be achieved by incorporating the unnatural amino acid 2,2,6,6-tetramethylpiperidine-N-oxyl-4-amino-4-carboxylic acid (TOAC, Fig. 1) [26,27]. While TOAC is a good substitute for the rare amino acid -aminoisobutyric acid that features in antibiotic peptaibols [29], it is an achiral amino acid with a tetrasubstituted C  atom and unusual preferences for a limited range of backbone dihedral angles.…”

Section: Labeling Strategy and Common Spin Labelsmentioning

confidence: 99%

Conformational dynamics and distribution of nitroxide spin labels

Jeschke

2013

Progress in Nuclear Magnetic Resonance Spectroscopy

136

115

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Long-range distance measurements based on paramagnetic relaxation enhancement (PRE) in NMR, quantification of surface water dynamics near biomacromolecules by Overhauser dynamic nuclear polarization (DNP) and sensitivity enhancement by solid-state DNP all depend on introducing paramagnetic species into an otherwise diamagnetic NMR sample. The species can be introduced by site-directed spin labeling, which offers precise control for positioning the label in the sequence of a biopolymer. However, internal flexibility of the spin label gives rise to dynamic processes that potentially influence PRE and DNP behavior and leads to a spatial distribution of the electron spin even in solid samples. Internal dynamics of spin labels and their static conformational distributions have been studied mainly by electron paramagnetic resonance spectroscopy and molecular dynamics simulations, with a large body of results for the most widely applied methanethiosulfonate spin label MTSL. These results are critically discussed in a unifying picture based on rotameric states of the group that carries the spin label. Deficiencies in our current understanding of dynamics and conformations of spin labeled groups and of their influence on NMR observables are highlighted and directions for further research suggested.

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“…To investigate the dynamics of the interaction between the SH2 domain and the longer peptides derived from FAK, peptides containing the spin-labeled amino acid TOAC (2,2,6,6,-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid) (19,20) were synthesized ( Table 1). The paramagnetic TOAC was introduced to determine whether the bound peptide assumes a single, well-defined orientation or samples several orientations.…”

Section: Dynamics Of Peptide Bindingmentioning

confidence: 99%

The Src SH2 domain interacts dynamically with the focal adhesion kinase binding site as demonstrated by paramagnetic nmr spectroscopy

Lindfors¹,

Drijfhout²,

Ubbink³

2012

IUBMB Life

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SummaryThe interaction between the tyrosine kinases Src and focal adhesion kinase (FAK) is a key step in signaling processes from focal adhesions. The phosphorylated tyrosine residue 397 in FAK is able to bind the Src SH2 domain. To establish the extent of the FAK binding motif, the binding affinity of the SH2 domain for phosphorylated and unphosphorylated FAKderived peptides of increasing length was determined and compared with that of the internal Src SH2 binding site. It is shown that the FAK peptides have higher affinity than the internal binding site and that seven negative residues adjacent to the core SH2 binding motif increase the binding constant 30-fold. A rigid spin-label incorporated in the FAK peptides was used to establish on the basis of paramagnetic relaxation enhancement whether the peptide-protein complex is well defined. A large spread of the paramagnetic effects on the surface of the SH2 domain suggests that the peptide-protein complex exhibits dynamics, despite the high affinity of the peptide. The strong electrostatic interaction between the positive side of the SH2 domain and the negative peptide results in a high affinity but may also favor a dynamic interaction.2012 IUBMB IUBMB Life, 64(6): 538-544, 2012

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A novel spin-labeled amino acid derivative for use in peptide synthesis: (9-fluorenylmethyloxycarbonyl)-2,2,6,6-tetramethylpiperidine-N-oxyl-4-amino-4-carboxylic acid

Cited by 151 publications

References 0 publications

Angiotensin II Binding to Angiotensin I–Converting Enzyme Triggers Calcium Signaling

Angiotensin II Binding to Angiotensin I–Converting Enzyme Triggers Calcium Signaling

Conformational dynamics and distribution of nitroxide spin labels

The Src SH2 domain interacts dynamically with the focal adhesion kinase binding site as demonstrated by paramagnetic nmr spectroscopy

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