Exploring side-chain diversity by submonomer solid-phase aza-peptide synthesis.
Organic letters
confidence
Key findings
Submonomer solid-phase synthesis of aza-GHRP-6 analogues; peptide 7a induced beta-turn conformation and 1000-fold improved CD36 receptor selectivity.
View source on PubMed (PMID 19606817) ↗
- Sample size
- 10 aza-analogues of GHRP-6
- Population
- In vitro peptide synthesis study
- Dosing
- Not reported
- Duration
- Not reported
- Route
- Not reported
- Blinding
- not_reported
- Controls
- not_reported
- Drug class
- GH secretagogue
Full abstract
Submonomer synthesis of aza-peptides featuring regioselective alkylation of peptide-bound aza-Gly residues provided ten aza-analogues of the Growth Hormone Releasing Peptide-6 (GHRP-6) in 15-42% yield and purity generally >or=90%. Circular dichroism demonstrated that azaPhe-peptide 7a induced a beta-turn conformation which may be responsible for its 1000-fold improvement in GHRP-6 selectivity for the CD36 receptor. This versatile method for making aza-peptides avoids solution-phase hydrazine synthesis and is well suited for studying side-chain-activity relationships of biologically active peptides.