PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Venom peptides”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1977

Bee venom peptides XVIII. Peptide-m and mcd-peptide: Isolation and characterization.

A simple method is described for the purification of peptide-M and MCD-peptide from bee venom. The steps are Sephadex G-50 gel filtration of pH 4.5 (Steps 1 and 2) and chromatography on silica gel (Steps 3 and 4). The peptides are homo geneous with respect to thin-layer chromatography, electrophoresis at pH 2.0, and amino acid analysis. Peptide-M contains 24 amino acid residues and has a calculated molecular weight of 2750.

Amino Acids↗
PubMed2026

Scorpion venom peptides: Novel therapeutic approaches for inflammatory and hepatic disorders.

Chronic hepatic disorders, such as metabolic dysfunction associated steatohepatitis (MASH), alcohol associated liver disease (ALD), and viral hepatitis (Hepatitis B virus [HBV]/Hepatitis C virus [HCV]), are primarily driven by persistent immune-mediated inflammation and hepatic stellate cell activation leading to fibrosis, yet conventional therapies lack tissue and molecular specificity. Scorpion venom peptides, refined through evolutionary selection, provide highly potent, target specific scaffolds capable of modulating intrahepatic inflammatory networks. Recent in vivo preclinical studies indicate that voltage gated potassium (Kv1.3) channel blocking peptides, such as BmKK2, significantly reduce macrophage activation and inhibit downstream cytokine production, effectively ameliorating diet-induced steatohepatitis and tissue scarring in murine models. Engineered hepatotropic candidates, such as Smp76 and Mucroporin-M1, demonstrate dual therapeutic functions: they neutralize extracellular Hepatitis C particles and suppress key host transcription factors necessary for Hepatitis B replication. This review systematically examines scorpion venom peptides organized by disease category, covering their historical development, structural classification into disulfide-bridged and non-disulfide-bridged families, ion channel specificity, hepatic anti-inflammatory and antiviral mechanisms, and translational challenges including nano-formulation delivery strategies and computational drug design. These target-specific peptides are ultimately positioned as promising molecular leads that may bridge targeted immunomodulation with the resolution of chronic, progressive liver injury.

Anti-inflammatory effects↗
PubMedDate not supplied

[Effect of bradkinin-potentiating snake venom peptides and C-terminal pentapeptide fragment of bradkinin on carboxypeptidase N and kiniase activities of human blood serum].

Effects of bradikinin-potentiating peptides (BPP5a and BPPB), which are identical to peptides from Bothrops jararaca and Agkistrodon halys blomhoffii snake venom, and pentapeptide C-terminal bradikinin fragment on carboxypeptidase N and kinase activities in human blood serum are studied. It is found that BPP5a and BPPB at concentrations of 5-10(-4) M and 2.5-10(-4) M respectively do not inhibit the hydrolysis of hippuryl-L-lysine and hippuryl-L-argininic acid by carboxypeptidase N and at a concentration of 2-10(-3) M they do not affect the rate of the release of C-terminal arginine residue from bradikinin. BPP5a and BPPB do not inhibit the kininase activity of diluted human blood serum in vitro. Unlike BPP5a and BPPB, C-terminal pentapeptide bradikinin fragment is a competitive inhibitor of carboxypeptidase N, and it inhibits (at a concentration of 5-10(-4) M) the hydrolysis of hippuryl-L-lysine and hippuryl-L-argininic acid by 50%. It also inhibits the hydrolysis of bradikinin with diluted human blood serum. BPP5a and BPPB have an inconstant constriction effect on isolated rat uterus at concentration exceeding 4-6 orders the concentration of bradikinin. BPP5a at concentrations from 4-10(-9) to 4-10(-8) g/ml increases the sensitivity of rat uterus in 1.6--2.0 times.

Animals↗
PubMed1977

Bradykinin potentiating and sensitizing activities of new synthetic analogues of snake venom peptides.

The structural requirements for prolonged residual ("sensitizing") activity in bradykinin-potentiating peptides (BPP's) were investigated through a study of seven synthetic BPP's including three not previously described: [Lys6]-BPP9a, [Gly6]potentiator B, and [Lys6,Gln8]potentiator B. The quantitation of the sensitizing activities in the isolated guinea pig ileum indicated that the structural requirements for bradykinin potentiation and for sensitization were not the same. The most potent sensitizers were potentiator B and [Lys6]-BPP9a.

Animals↗
PubMed2026

Sex- and development-specific transcriptomic profiling of venom and silk genes in the wolf spider Pardosa astrigera provides insights into ecological adaptation and predatory strategies.

Spider venom and silk glands are two major secretory systems that contribute to prey capture, defense, and reproduction, but their sex- and development-specific molecular regulation in wandering wolf spiders remains poorly understood. Here, the transcriptome of Pardosa astrigera, an important agricultural natural enemy in China, revealed significant sex- and development-associated molecular differentiation among adult females, adult males, and spiderlings. A total of 100,025 unigenes were obtained, of which 23,852 were functionally annotated, providing a comprehensive transcriptomic resource for this species. Differential expression patterns showed marked variation among groups, with 531, 1792, and 832 DEGs detected in PAF vs PAS, PAM vs PAS, and PAF vs PAM, respectively. These genes were mainly associated with metabolic, oxidation-reduction, cuticle development, MAPK signaling, and lysosome pathways. Fifteen co-expression modules revealed distinct expression patterns. The turquoise, pink, yellow, and red modules were development-related, whereas the blue module was male-biased. Venom- and spidroin-related genes were distributed across multiple modules, suggesting coordinated regulation. Overall, 42 venom peptides, 21 venom proteins, and 11 spidroins were identified. Representative genes showed strongly biased expression, including spiderling-biased U3_Pp1a and U5_Pp1e, female-biased U4_Pp1a, and male-biased SMase D_108750 and PaTuSp_108466. These findings reveal sex- and development-biased expression patterns of venom- and silk-related candidate genes in P. astrigera and may provide molecular insights into ecological adaptation and predatory strategies in wandering wolf spiders.

Animals↗
PubMed1977

[Basic peptides in bee venom, III. Synthesis of peptide fragments from the sequence of the mast-cell-degranulating peptide (author's transl)].

The synthesis by conventional methods of the following three peptides is described: MCD(8-11) Boc-His(Trt)-Val-Ile-Lys(Z) (III) MCD(5-7) Boc-Cys(SiPr)-Lys(Z)-Arg(Tos) (IV) and MCD(1-4) Boc-Ile-Lys(Z)-Cys(Trt)-Asn(Mbh) (V). These peptides are fragments of the mast cell degranulating peptide from bee venom. The purity of the fragments synthesized was examined by thin-layer chromatography, amino acid and elementary analysis. Including the fragments Boc-Lys(Z)-Ile-Cys(SiPr)-Gly-Lys(Z) (I) and Boc-Pro-His(Trt)-Ile-Cys(Trt)-Arg(Tos) (II), which were described earlier, the synthesis of the mast-cell-degranulating peptide on a polyethylene-asparagine support appears possible.

Amino Acid Sequence↗
PubMed1978

The structures of some peptides from bee venom.

The sequences are given of two peptides (secapin and melittin F) whose isolation from the venom of the common European honey bee (Apis mellifera) has previously been described [Gauldie et al. (1976) Eur. J. Biochem. 61, 369--376]. Some structural studies on the known peptide 401 (MCD peptide) are described. The positions of the two disulphide bridges in peptide 401 have been determined by (an essentially) novel method.

Amino Acid Sequence↗
PubMed1977

[Histamine-liberating action of MCD-peptide from bee venom].

Histamine release (HR) from the isolated rat mast cells induced by MCD-peptide, mellitin (from the Apis mellifica venom) and compound 48/80 was studied. The dose-response curve, the latent period and temperature dependence of HR induced by MCD-peptide were similar to those of HR induced by compound 48/80. The HR induced by MCD-peptide proved to be an energy-dependent process that was independent of cyclic adenosine-3',5'-monophosphate.

Animals↗
PubMed1979

Snake venoms. The amino-acid sequence of protein S2C4 from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom.

A major component (S2C4) was purified from Jameson's mamba by gel filtration on Sephadex G-50 and ion-exchange chromatography on CM-cellulose. Protein S2C4 comprises 62 amino acid residues including 8 half-cystine residues. The complete amino acid sequence of the protein has been established. The sequence and the invariant amino acid residues of protein S2C4 resemble a short neurotoxin, a long neurotoxin, a cytotoxin and an angusticeps type protein. However, the position of its four disulphide bridges differs from those encountered in a short neurotoxin or a cytotoxin. Mixtures of protein S2C4 and angusticeps type proteins revealed a marked synergistic effect, in that their toxicity in combination was greater than the sum of their individual toxicities.

Amino Acid Sequence↗
PubMed1978

Snake venoms. The amino-acid sequence of protein S5C4 from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom.

A major component (S5C4) was purified from Jameson's mamba by gel filtration on Sephadex G-50 and by ion-exchange chromotography on CM-cellulose. Protein S5C4 contains 60 amino acid residues and is cross-linked by four intrachain disulphide bridges. The complete primary structure of the protein has been elucidated. The toxicities, the immunochemical properties, the sequence and the invariant amino acid residues of protein S5C4 resemble subgroup II of the angusticeps-type proteins.

Amino Acid Sequence↗