Structure-Activity Studies of Analogues of Blomhotin Mediating Contraction of Rat Fundus

Blomhotin is a novel peptide (pGlu1-Gly2-Arg3-Pro4-Pro5-Gly6-Pro7-Pro8-Ile9-Pro10-Arg11) which has been isolated from the venom of Agkistrodon halys blomhoffii and exhibits contractile activity on rat stomach fundus. We carried out a structure-activity study of blomhotin and its related peptides, an...

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Published inBiological & pharmaceutical bulletin Vol. 23; no. 11; pp. 1379 - 1381
Main Authors YANOSHITA, Ryohei, IWASAKI, Eyu, KAMBE, Terumi, SAMEJIMA, Yuji
Format Journal Article
LanguageEnglish
Published Tokyo The Pharmaceutical Society of Japan 01.11.2000
Maruzen
Japan Science and Technology Agency
Subjects
Animals
Biological and medical sciences
blomhotin
Crotalid Venoms - agonists
Crotalid Venoms - chemistry
Crotalid Venoms - pharmacology
Gastric Fundus - drug effects
General pharmacology
In Vitro Techniques
Male
Medical sciences
Muscle
Muscle Contraction - drug effects
Muscle, Smooth - drug effects
peptide
Pharmacology. Drug treatments
Photoaffinity Labels
Physicochemical properties. Structure-activity relationships
Pyrrolidonecarboxylic Acid - analogs & derivatives
rat fundus
Rats
Rats, Wistar
smooth muscle
Structure-Activity Relationship
Stomach
Peptides
Rat
Digestive system
Rodentia
Animal origin
Smooth muscle
Muscle contraction
In vitro
Ophidia
Vertebrata
Biological fixation
Mammalia
Structure activity relation
Analog
Animal
Venom
Gastric fundus
Peptidergic receptor
Reptilia
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Summary:Blomhotin is a novel peptide (pGlu1-Gly2-Arg3-Pro4-Pro5-Gly6-Pro7-Pro8-Ile9-Pro10-Arg11) which has been isolated from the venom of Agkistrodon halys blomhoffii and exhibits contractile activity on rat stomach fundus. We carried out a structure-activity study of blomhotin and its related peptides, and the findings suggested that the N-terminal portion of blomhotin is mainly responsible for affinity for the blomhotin receptor, whereas the C-terminal portion of blomhotin, Pro-Ile-Pro-Arg, is responsible for complete activation of the blomhotin receptor in the rat stomach fundus. In particular, the amino acids at positions 9 and 11 of blomhotin appear to be essential for binding and intrinsic activity. Using knowledge gained from this structure-activity analysis, we have identified photoactive blomhotin analogues that have sufficient biological activity to probe the target molecule of blomhotin.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.23.1379