The measurement of H-1 off-resonance nonselective relaxation rates (R-theta,(ns)) has been recently proposed as an effective method to probe peptide self-recognition, opening new perspectives in the understanding of the prefibrillization oligomerization processes in amylodogenesis. However, a full analysis and parametric optimization of the NMR experiments designed to measure R-theta,R-ns relaxation rates is still missing. Here we analyze the dependence of the R-theta,R-ns rates upon three critical parameters: the tilt angle of the effective field during the spin lock, the static magnetic field, and finally the repetition delay. Our analysis reveals that the tilt angle theta = 35.5 degrees not only minimizes spin-diffusion, but also avoids experimental artifacts such as J-transfer and poor adiabaticity. In addition, we found that when the dominant relaxation mechanism is caused by uncorrelated pairwise H-1 dipole-H-1 dipole interactions the R-35.5 degrees,R-ns rate is not significantly affected by static field variations, suggesting a wide applicability of the H-1 off-resonance nonselective relaxation experiment. Finally, we show that the self-recognition maps based on the comparative analysis of the R-35.5 degrees,R-ns rates can tolerate decreases in the interscan delays without significantly compromising the identification of critical self-association loci. These considerations not only provide a better understanding of the H-1 off-resonance nonselective relaxation, but they also serve as guidelines for the optimal setup of this experiment.