Structural requirements for the edema-inducing and hemolytic activities of mastoparan B isolated from the hornet (Vespa basalis) venom

C. L. Ho, Y. L. Lin, W. C. Chen, L. L. Hwang, H. M. Yu, K. T. Wang

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Mastoparan B (MP-B) is a cationic tetradecapeptide isolated from the black-bellied hornet (Vespa basalis) venom. It has a primary structure (LKLKSIVSWAKKVL-CONH2,) distinct from other vespine mastoparans. The peptide caused a dose-dependent swelling in rat hind paw and showed a potent hemolytic activity in guinea pig red blood cells. Studies on the structure activity relationship of the peptide showed that replacing lysine at position 2 (Lys2) by asparagine (Asn) in the MP-B sequence caused about 40% decrease in its edema-inducing activity at 50 μg/paw and 90% decrease in hemolytic activity at 30 μM of the peptide, while the same substitution at Lys4 did not cause a significant change in either activity. Replacing either Lys11 or Lys12 by leucine (Leu) caused little or no decrease in the edema-inducing and hemolytic activities. Decreases in both activities were observed when both Lys11 and Lys12 were replaced by Leu. On the other hand, replacing tryptophan at position 9 (Trp9 by tyrosine or phenylalanine in MP-B sequence almost abolished its hemolytic activity, while the edema-inducing activity was only partially inhibited. Circular dichroism spectra of the peptides measured in 20% trifluoro- ethanol revealed that substitution of Lys and Trp did not cause a significant change in the conformation of MP-B. It appears that Lys2 is crucial for both hemolytic and edema-inducing activities of MP-B, while Trp9 is of special importance to the hemolytic activity of MP-B. Lys11 and Lys12 in MP-B probably play a lesser role in both activities.

Original languageEnglish
Pages (from-to)1027-1035
Number of pages9
JournalToxicon
Volume34
Issue number9
DOIs
Publication statusPublished - Sep 1996
Externally publishedYes

Fingerprint

Wasp Venoms
Wasps
Venoms
Edema
Leucine
Peptides
Substitution reactions
Asparagine
Structure-Activity Relationship
Circular Dichroism
Phenylalanine
Tryptophan
Lysine
Tyrosine
Swelling
Conformations
Rats
Guinea Pigs
Blood
Ethanol

ASJC Scopus subject areas

  • Toxicology

Cite this

Structural requirements for the edema-inducing and hemolytic activities of mastoparan B isolated from the hornet (Vespa basalis) venom. / Ho, C. L.; Lin, Y. L.; Chen, W. C.; Hwang, L. L.; Yu, H. M.; Wang, K. T.

In: Toxicon, Vol. 34, No. 9, 09.1996, p. 1027-1035.

Research output: Contribution to journalArticle

Ho, C. L. ; Lin, Y. L. ; Chen, W. C. ; Hwang, L. L. ; Yu, H. M. ; Wang, K. T. / Structural requirements for the edema-inducing and hemolytic activities of mastoparan B isolated from the hornet (Vespa basalis) venom. In: Toxicon. 1996 ; Vol. 34, No. 9. pp. 1027-1035.
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abstract = "Mastoparan B (MP-B) is a cationic tetradecapeptide isolated from the black-bellied hornet (Vespa basalis) venom. It has a primary structure (LKLKSIVSWAKKVL-CONH2,) distinct from other vespine mastoparans. The peptide caused a dose-dependent swelling in rat hind paw and showed a potent hemolytic activity in guinea pig red blood cells. Studies on the structure activity relationship of the peptide showed that replacing lysine at position 2 (Lys2) by asparagine (Asn) in the MP-B sequence caused about 40{\%} decrease in its edema-inducing activity at 50 μg/paw and 90{\%} decrease in hemolytic activity at 30 μM of the peptide, while the same substitution at Lys4 did not cause a significant change in either activity. Replacing either Lys11 or Lys12 by leucine (Leu) caused little or no decrease in the edema-inducing and hemolytic activities. Decreases in both activities were observed when both Lys11 and Lys12 were replaced by Leu. On the other hand, replacing tryptophan at position 9 (Trp9 by tyrosine or phenylalanine in MP-B sequence almost abolished its hemolytic activity, while the edema-inducing activity was only partially inhibited. Circular dichroism spectra of the peptides measured in 20{\%} trifluoro- ethanol revealed that substitution of Lys and Trp did not cause a significant change in the conformation of MP-B. It appears that Lys2 is crucial for both hemolytic and edema-inducing activities of MP-B, while Trp9 is of special importance to the hemolytic activity of MP-B. Lys11 and Lys12 in MP-B probably play a lesser role in both activities.",
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