New proctolin analogs modified in position 3 of peptide chain--synthesis and their biological evaluation.
Six proctolin analogs modified in position 3 of peptide chain such as Arg-Tyr-X-Pro-Thr where X = Gly (1), Val (2), Pro (3), Thr (4), Acp (1-aminocyclopentane-1-carboxylic acid residue) (5), and Ach (1-aminocyclohexane-1-carboxylic acid residue) (6) were synthesized by liquid-phase method. Biological effects of the pentapeptides (1-6) were examined in cardiostimulatory test in vitro in respect to two insect species: American cockroach (Periplaneta americana L.) and yellow mealworm (Tenebrio molitor L.). Results thus obtained pointed out that the presence of L-leucine in the position 3 of proctolin skeleton plays important role in its cardiotropic activity in insects.
Konopińska
D
D
Institute of Chemistry, University of Wrocław, Poland.
Rosiński
G
G
Sobótka
W
W
D000595:Amino Acid Sequence; D000818:Animals; D002316:Cardiotonic Agents / Q000737:chemistry / Q000494:pharmacology*; D006339:Heart Rate / Q000187:drug effects*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009479:Neuropeptides; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology*; D010526:Periplaneta / Q000187:drug effects; D013329:Structure-Activity Relationship; D013712:Tenebrio / Q000187:drug effects
D002316:Cardiotonic Agents; D009479:Neuropeptides; D009842:Oligopeptides; C011536:proctolin