Schematic structure of the tripeptide Arg-Gly-Asp (RGD) with the labeling of the carbons of the amino acid residues.
NMR peak assignment at 500 MHz of the protons of RGD at a 5 mM concentration in D2O at 298 K. (a) 1H NMR spectrum with the integrals of the various splitting patterns. (b) 1H–1H gradient COSY spectrum of RGD using a 2048 × 512 matrix over a 4500 Hz spectral width.
Space-filling models of RGD, D6MF, and HOD interacting with Lnttha3−.
1H NMR spectra at 298K and 400 MHz of HOD, RGD, and tBuOD in D2O solutions containing no complex (diamagnetic blank solution), 1.45 mM Tbttha3−, and 3.9 mM Erttha3−. The resonance of the tBuOD reference protons is set to δ tBuOD = 1.11 ppm in the three solutions.
1H NMR spectra at 298 K and 200 MHz of RGD in the diamagnetic blank D2O solution S blk and paramagnetic D2O solutions S TbEr and S TbErGd containing Tbttha3−, Erttha3−, and Gdttha3− at appropriate concentrations reported in Table I. The resonance of the HOD protons is set to δ HOD = 4.65 ppm in the three solutions.
Parallel 1H NMR determination at 298 K and 400 MHz of the effective magnetic moment μ eff, Ln of Lnttha3− in D2O solutions placed in capillary tubes and containing tBuOD reference protons with increasing concentrations c Ln of complex. (a) Tbttha3−: c Tb = 0, 5.79, and 11.93 mM. (b) Erttha3−: c Er = 0, 5.62, and 11.95 mM.
Experimental relaxation rates and relaxivities at 298 K and 200 MHz of the various chemically equivalent groups of protons of N,N-dimethyl-D6-formamide (D6MF), HOD, and Arg-Gly-Asp (RGD) in a diamagnetic blank solution S blk and two paramagnetic solutions S TbEr ( = 3.17 mM, = 8.38 mM, no Gd3+ complex) and S TbErGd (c Tb = 3.10 mM, c Er = 8.21 mM, c Gd = 0.294 mM).
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