A novel serine protease inhibitor from Bungarus fasciatus venom

Jia, L. K.; Yang, Hailong; Yu, Haining; Gao, Weikai; Lai, Ren; Liu, Jingze; Liang, Xingcai

doi:10.1016/j.peptides.2007.11.013

Cited by 50 publications

(30 citation statements)

References 21 publications

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“…Their divergent venom peptides are still waiting for exploitation in drug development. Scorpion-derived Kunitz-type venom peptide SdPI is a potent trypsin inhibitor with a K i value of 1.6×10 −7 M. Compared with other Kunitz-type venom peptides, SdPI has greater trypsin inhibitory activity than snake-derived bungaruskunin, but weaker activity than sea anemone-derived kalicludines and spider-derived HWTX-XI (Table 2) [6], [7], [29]. Although more study is needed to explain why these different Kunitz-type venom peptides vary in activity, they are nonetheless potential candidates for engineering more specific inhibitors against trypsin.…”

Section: Discussionmentioning

confidence: 99%

“…The initial rate of p -nitroanilide ( p NA) production was monitored continuously at 405 nm for 5 min at 25°C. The inhibitory activity of rSdPI was determined by setting the initial velocity with protease alone as 100% [29]. Lineweaver–Burk plots (1/V vs. 1/[S]) were used to determine the K m /V max values of trypsin activity on N α -benzoyl-L-arginine 4-nitroanilide in the presence of different inhibitor concentration.…”

Section: Methodsmentioning

confidence: 99%

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SdPI, The First Functionally Characterized Kunitz-Type Trypsin Inhibitor from Scorpion Venom

et al. 2011

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BackgroundKunitz-type venom peptides have been isolated from a wide variety of venomous animals. They usually have protease inhibitory activity or potassium channel blocking activity, which by virtue of the effects on predator animals are essential for the survival of venomous animals. However, no Kunitz-type peptides from scorpion venom have been functionally characterized.Principal FindingsA new Kunitz-type venom peptide gene precursor, SdPI, was cloned and characterized from a venom gland cDNA library of the scorpion Lychas mucronatus. It codes for a signal peptide of 21 residues and a mature peptide of 59 residues. The mature SdPI peptide possesses a unique cysteine framework reticulated by three disulfide bridges, different from all reported Kunitz-type proteins. The recombinant SdPI peptide was functionally expressed. It showed trypsin inhibitory activity with high potency (Ki = 1.6×10−7 M) and thermostability.ConclusionsThe results illustrated that SdPI is a potent and stable serine protease inhibitor. Further mutagenesis and molecular dynamics simulation revealed that SdPI possesses a serine protease inhibitory active site similar to other Kunitz-type venom peptides. To our knowledge, SdPI is the first functionally characterized Kunitz-type trypsin inhibitor derived from scorpion venom, and it represents a new class of Kunitz-type venom peptides.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

SdPI, The First Functionally Characterized Kunitz-Type Trypsin Inhibitor from Scorpion Venom

et al. 2011

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“…Our previous studies provided the first evidence of the fibrin(ogen)olytic activity of bumblebee venom serine proteases, which act as prothrombin activators, thrombin-like proteases, and plasmin-like proteases [13], [14]. Although several Kunitz-type serine protease inhibitors have been reported to be present in snake venom [7], [15]–[17], the role of serine protease inhibitors in bee venom remains unknown.…”

Section: Introductionmentioning

confidence: 99%

Antifibrinolytic Role of a Bee Venom Serine Protease Inhibitor That Acts as a Plasmin Inhibitor

et al. 2012

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Bee venom is a rich source of pharmacologically active substances. In this study, we identified a bumblebee (Bombus ignitus) venom Kunitz-type serine protease inhibitor (Bi-KTI) that acts as a plasmin inhibitor. Bi-KTI showed no detectable inhibitory effect on factor Xa, thrombin, or tissue plasminogen activator. In contrast, Bi-KTI strongly inhibited plasmin, indicating that it acts as an antifibrinolytic agent; however, this inhibitory ability was two-fold weaker than that of aprotinin. The fibrin(ogen)olytic activities of B. ignitus venom serine protease (Bi-VSP) and plasmin in the presence of Bi-KTI indicate that Bi-KTI targets plasmin more specifically than Bi-VSP. These findings demonstrate a novel mechanism by which bumblebee venom affects the hemostatic system through the antifibrinolytic activity of Bi-KTI and through Bi-VSP-mediated fibrin(ogen)olytic activities, raising interest in Bi-KTI and Bi-VSP as potential clinical agents.

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“…Functionally, many Kunitz-type toxins have protease and/or potassium channel inhibiting properties. For example, Kunitz-type toxin bungaruskunin, isolated from snake venom, is a serine protease inhibitor (22), but ␣-dentrotoxin, ␦-dentrotoxin, dentrotoxin K, and dentrotoxin I, also from snake venom, are potent Kv1.1 channel inhibitors (21). Kunitz-type toxins HWTX-XI from spider and APEKTx1, AKC1, AKC2, and AKC3 from sea anemone are bifunctional toxin peptides with both protease and potassium channel-inhibiting properties (20,23,24).…”

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confidence: 99%

Hg1, Novel Peptide Inhibitor Specific for Kv1.3 Channels from First Scorpion Kunitz-type Potassium Channel Toxin Family

Chen

Yang

et al. 2012

Journal of Biological Chemistry

112

101

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Background:The potassium channel inhibitory activity of scorpion Kunitz-type toxins has not yet been determined. Results: We identified the first scorpion Kunitz-type potassium channel toxin family with three groups and seven members. Conclusion: A novel peptide, Hg1, specific for Kv1.3 channel, was found. Significance: Kunitz-type toxins are a new source to screen and design potential peptides for diagnosing and treating Kv1.3-mediated autoimmune diseases.

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A novel serine protease inhibitor from Bungarus fasciatus venom

Cited by 50 publications

References 21 publications

SdPI, The First Functionally Characterized Kunitz-Type Trypsin Inhibitor from Scorpion Venom

SdPI, The First Functionally Characterized Kunitz-Type Trypsin Inhibitor from Scorpion Venom

Antifibrinolytic Role of a Bee Venom Serine Protease Inhibitor That Acts as a Plasmin Inhibitor

Hg1, Novel Peptide Inhibitor Specific for Kv1.3 Channels from First Scorpion Kunitz-type Potassium Channel Toxin Family

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