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A Novel Factor Xa-Inhibiting Peptide from Centipedes Venom.

Kong Y, Shao Y, Chen H, Ming X, Wang JB, Li ZY, Wei JF - Int J Pept Res Ther (2013)

Bottom Line: It prolonged the partial thromboplastin time and prothrombin time in both in vitro and ex vivo assays.It also significantly prolonged whole blood clotting time and bleeding time in mice.This is the first report that an FXa inhibiting peptide was isolated from centipedes venom.

View Article: PubMed Central - PubMed

Affiliation: School of Life Science & Technology, China Pharmaceutical University, 24 Tong Jia Xiang, Nanjing, 210009 People's Republic of China ; State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing, 210009 People's Republic of China.

ABSTRACT
Centipedes have been used as traditional medicine for thousands of years in China. Centipede venoms consist of many biochemical peptides and proteins. Factor Xa (FXa) is a serine endopeptidase that plays the key role in blood coagulation, and has been used as a new target for anti-thrombotic drug development. A novel FXa inhibitor, a natural peptide with the sequence of Thr-Asn-Gly-Tyr-Thr (TNGYT), was isolated from the venom of Scolopendra subspinipes mutilans using a combination of size-exclusion and reverse-phase chromatography. The molecular weight of the TNGYT peptide was 554.3 Da measured by electrospray ionization mass spectrometry. The amino acid sequence of TNGYT was determined by Edman degradation. TNGYT inhibited the activity of FXa in a dose-dependent manner with an IC50 value of 41.14 mg/ml. It prolonged the partial thromboplastin time and prothrombin time in both in vitro and ex vivo assays. It also significantly prolonged whole blood clotting time and bleeding time in mice. This is the first report that an FXa inhibiting peptide was isolated from centipedes venom.

No MeSH data available.


Purification of TNGYT from centipede venom. aS. subspinipes mutilans venom was separated by Sephadex G-50 column. b The faction 2 after Sephadex G-50 column was separated by RP-HPLC on a C18 column. c The fraction C-3 after RP-HPLC on a C18 column was separated by another C18 column. The final purified peptide was designated as TNGYT
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Fig1: Purification of TNGYT from centipede venom. aS. subspinipes mutilans venom was separated by Sephadex G-50 column. b The faction 2 after Sephadex G-50 column was separated by RP-HPLC on a C18 column. c The fraction C-3 after RP-HPLC on a C18 column was separated by another C18 column. The final purified peptide was designated as TNGYT

Mentions: The crude venom was separated into six fractions by Sephadex G50 column (Fig. 1a). Fractions 1, 2 and 3 showed aPTT and PT activity. Fraction 2 was then separated by RP-HPLC on a Lichrospher C18 column (Fig. 1b). Fraction 2–6 showed aPTT and PT activity. This active fraction was then purified by another C18 column (Fig. 1c) to give the final purified peptide.Fig. 1


A Novel Factor Xa-Inhibiting Peptide from Centipedes Venom.

Kong Y, Shao Y, Chen H, Ming X, Wang JB, Li ZY, Wei JF - Int J Pept Res Ther (2013)

Purification of TNGYT from centipede venom. aS. subspinipes mutilans venom was separated by Sephadex G-50 column. b The faction 2 after Sephadex G-50 column was separated by RP-HPLC on a C18 column. c The fraction C-3 after RP-HPLC on a C18 column was separated by another C18 column. The final purified peptide was designated as TNGYT
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3824214&req=5

Fig1: Purification of TNGYT from centipede venom. aS. subspinipes mutilans venom was separated by Sephadex G-50 column. b The faction 2 after Sephadex G-50 column was separated by RP-HPLC on a C18 column. c The fraction C-3 after RP-HPLC on a C18 column was separated by another C18 column. The final purified peptide was designated as TNGYT
Mentions: The crude venom was separated into six fractions by Sephadex G50 column (Fig. 1a). Fractions 1, 2 and 3 showed aPTT and PT activity. Fraction 2 was then separated by RP-HPLC on a Lichrospher C18 column (Fig. 1b). Fraction 2–6 showed aPTT and PT activity. This active fraction was then purified by another C18 column (Fig. 1c) to give the final purified peptide.Fig. 1

Bottom Line: It prolonged the partial thromboplastin time and prothrombin time in both in vitro and ex vivo assays.It also significantly prolonged whole blood clotting time and bleeding time in mice.This is the first report that an FXa inhibiting peptide was isolated from centipedes venom.

View Article: PubMed Central - PubMed

Affiliation: School of Life Science & Technology, China Pharmaceutical University, 24 Tong Jia Xiang, Nanjing, 210009 People's Republic of China ; State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing, 210009 People's Republic of China.

ABSTRACT
Centipedes have been used as traditional medicine for thousands of years in China. Centipede venoms consist of many biochemical peptides and proteins. Factor Xa (FXa) is a serine endopeptidase that plays the key role in blood coagulation, and has been used as a new target for anti-thrombotic drug development. A novel FXa inhibitor, a natural peptide with the sequence of Thr-Asn-Gly-Tyr-Thr (TNGYT), was isolated from the venom of Scolopendra subspinipes mutilans using a combination of size-exclusion and reverse-phase chromatography. The molecular weight of the TNGYT peptide was 554.3 Da measured by electrospray ionization mass spectrometry. The amino acid sequence of TNGYT was determined by Edman degradation. TNGYT inhibited the activity of FXa in a dose-dependent manner with an IC50 value of 41.14 mg/ml. It prolonged the partial thromboplastin time and prothrombin time in both in vitro and ex vivo assays. It also significantly prolonged whole blood clotting time and bleeding time in mice. This is the first report that an FXa inhibiting peptide was isolated from centipedes venom.

No MeSH data available.