In docking models, GHRP‑6 and the other studied peptides showed superposition of their N-terminal and first aromatic residue.
In plain wordsIn computer models, GHRP‑6 and other peptides showed overlapping positions of their N-terminal and first aromatic residue.
- Peptide
- GHRP-6
- Outcome
- Not applicableDocked peptide orientation
- Study
n: not reported in source
GHS-R1a molecular docking and dynamics- Outcome group
- Receptor activity and mechanism · Pharmacology
Source sentences
Docking was used to estimate peptide orientations in the binding site of the best model, observing a superposition of its N-terminal and its first aromatic residue.
1 context sentence(design, population, supporting numbers)
In this work, an in silico strategy was developed for describing and assessing the binding modes of A228 and A233 to GHS-R1a (ghrelin receptor) comparing it with ghrelin and GHRP-6 peptides.
In this study, GHRP-6 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking GHRP-6.