GHRH-receptor structure and analytical detection of tesamorelin
Tesamorelin is a stabilized growth hormone-releasing hormone analog suited to research on GHRH-receptor recognition, sequence–activity relationships, and mass-spectrometric detection.
Overview
Tesamorelin is an analog of the 44-amino-acid growth hormone-releasing hormone sequence. As with other GHRH-family peptides, its N-terminal residues are central to receptor activation, while modifications elsewhere can alter stability and experimental handling.
Cryo-electron microscopy has resolved the GHRH–GHRH receptor–Gs complex, providing a structural framework for peptide recognition. Earlier structure–activity work used systematic substitutions and in vitro assays to identify residues that influence receptor activation. Analytical studies have also included tesamorelin in multi-analyte LC-HRMS/MS detection workflows.
These sources support receptor-structure, sequence–activity, and analytical-method research. They do not mean a VIVO material was evaluated in the cited studies, and they do not establish safety, efficacy, dosing, administration, or an expected outcome in humans or animals.
References
Peer-reviewed sources for the research summarised above. Vivo summarises published, third-party science and does not conduct or sponsor this research.
- Dong M, et al. (2020). Structural basis for activation of the growth hormone-releasing hormone receptor. Nature Communications; 11:5205. View source ↗
- Campbell RM, Bongers J, Felix AM (1995). Rational design, synthesis, and biological evaluation of novel growth hormone-releasing factor analogues. Biopolymers; 37(1):67–88. View source ↗
- Thomas A, Delahaut P, Krug O, et al. (2016). Identification of Geref, CJC-1293, CJC-1295, and tesamorelin by immunoaffinity purification and LC-HRMS/MS. Analytical and Bioanalytical Chemistry; 408:4859–4871. View source ↗