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Peptide T is a synthetic octapeptide fragment, which corresponds to the region 185–192 of the gp120 HIV coat protein and functions as a viral entry inhibitor. In this work, a folding molecular dynamics simulation of peptide T in a membrane‐mimicking (DMSO) solution was performed with the aim of characterizing the peptide's structural and dynamical properties. We show that peptide T is highly flexible and dynamic. The main structural characteristics observed were rapidly interconverting short helical stretches and turns, with a notable preference for the formation of  β ‐turns. The simulation also indicated that the C‐terminal part appears to be more stable than the rest of the peptide, with the most preferred conformation for residues 5–8 being a  β ‐turn. In order to validate the accuracy of the simulations, we compared our results with the experimental NMR data obtained for the T‐peptide in the same solvent. In agreement with the simulation, the NMR data indicated the presence of a preferred structure in solution that was consistent with a  β ‐turn comprising the four C‐terminal residues. An additional comparison between the experimental and simulation‐derived chemical shifts also showed a reasonable agreement between experiment and simulation, further validating the simulation‐derived structural characterization of the T‐peptide. We conclude that peptide folding simulations produce physically relevant results even when performed with organic solvents that were not part of the force field parameterization procedure.

Folding molecular dynamics simulation of T‐peptide, a HIV viral entry inhibitor: Structure, dynamics, and comparison with the experimental data