Journal
MOLECULAR DIVERSITY
Volume 17, Issue 1, Pages 19-31Publisher
SPRINGER
DOI: 10.1007/s11030-012-9399-5
Keywords
Peptidomimetic; Endomorphin-2; Beta-amino acid; Opioid receptor; Molecular modelling; Molecular docking
Categories
Funding
- National Scientific Research Fund, Budapest, Hungary [OTKA CK-78566]
Ask authors/readers for more resources
This study reports on new pharmacologically active endomorphin-2 analogues, incorporating beta (2)-hPhe, beta (3)-hPhe and beta (3)-hTic unnatural amino acids in the place of the Phe(3)-Phe(4)residues. Such alpha, beta-hybrid analogues were designed to exploit the great potential of beta-amino acids in generating conformational variation at the key positions 3 and 4, with the aim of evaluating the effect on the opioid binding affinity. Ligand-stimulated binding assays indicated that some analogues retained a significant affinity, especially for the delta receptor. H-1 NMR and molecular modelling suggested the predominance of bent structures for all compounds. The molecular docking with the mu-opioid receptor model was also performed, highlighting a common binding mode for active compounds and helping to rationalize the observed structure-activity data.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available