[Conformation-activity relations of dermorphin and its pentapeptide analogs].
Low-energy peptide backbone structures of dermorphin (DM), amide of its N-terminal pentapeptide (DM 1-5) and DM 1-5 analogues with substitutions of Gly4 for Leu, D-Gln, Aal or Tal were determined by energy calculations. The above analogues were shown to possess different affinities toward opiate receptors of mu-type. The comparison of low-energy backbone structures of DM, DM 1-5 and its analogues resulted in development of the dermorphin "biologically active" conformation being characteristic of its binding with mu-type receptors. The specific binding of dermorphin to this receptor apparently depends on the conformation of the whole N-terminal pentapeptide.
Shenderovich
M D
MD
Liepinia
I T
IT
Nikiforovich
G V
GV
Sumbatian
N V
NV
Korshunova
G A
GA
Shvachkin
Iu P
IuP
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D018847:Opioid Peptides; D011487:Protein Conformation; D011957:Receptors, Opioid / Q000378:metabolism; D017450:Receptors, Opioid, mu; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D018847:Opioid Peptides; D011957:Receptors, Opioid; D017450:Receptors, Opioid, mu; C030058:dermorphin
Konformatsionno-funktsional'nye otnosheniia dermorfina i ego pentapeptidnykh analogov.