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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.


The molecular mass of TNGYT determined by ESI–MS. The molecular mass of purified TNGYT is 554.3 Da
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Fig2: The molecular mass of TNGYT determined by ESI–MS. The molecular mass of purified TNGYT is 554.3 Da

Mentions: The molecular mass of the purified peptide was determined to be 554.3 Da by ESI-MS (Fig. 2) and the primary structure was identified as Thr-Asn-Gly-Tyr-Thr (TNGYT) by Edman degradation. The molecular mass of TNGYT by ESI-MS matched the theoretical molecular mass (554.6 Da) deduced from amino acid sequence of TNGYT. By BLAST (http://blast.ncbi.nlm.nih.gov/) search, the peptide showed no similarity with any other known peptides or proteins in S. subspinipes mutilans (taxid: 251420). Although a few proteins from Streptococcus parasanguinis and Leptosphaeria maculans contained the fragment TNGYT, there was no single peptide fragment as TNGYT in the protein or peptide database.Fig. 2


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)

The molecular mass of TNGYT determined by ESI–MS. The molecular mass of purified TNGYT is 554.3 Da
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

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

Fig2: The molecular mass of TNGYT determined by ESI–MS. The molecular mass of purified TNGYT is 554.3 Da
Mentions: The molecular mass of the purified peptide was determined to be 554.3 Da by ESI-MS (Fig. 2) and the primary structure was identified as Thr-Asn-Gly-Tyr-Thr (TNGYT) by Edman degradation. The molecular mass of TNGYT by ESI-MS matched the theoretical molecular mass (554.6 Da) deduced from amino acid sequence of TNGYT. By BLAST (http://blast.ncbi.nlm.nih.gov/) search, the peptide showed no similarity with any other known peptides or proteins in S. subspinipes mutilans (taxid: 251420). Although a few proteins from Streptococcus parasanguinis and Leptosphaeria maculans contained the fragment TNGYT, there was no single peptide fragment as TNGYT in the protein or peptide database.Fig. 2

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.