Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom

Syed Abid Ali, Stanka Stoeva, Jürgen Schütz, Rakez Kayed, Atiya Abassi, Zafar H. Zaidi, Wolfgang Voelter

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

The primary structures of four low molecular mass peptides (Bs 6, 8, 10 and 14) from scorpion Buthus sindicus were elucidated via combination of Edman degradation and matrix-assisted laser desorption ionization mass spectrometry. Bs 8 and 14 are cysteine-rich, thermostable peptides composed of 35-36 residues with molecular weights of 3.7 and 3.4 kDa, respectively. These peptides show close sequence homologies (55-78%) with other scorpion chlorotoxin-like short-chain neurotoxins (SCNs) containing four intramolecular disulfide bridges. Despite the sequence variation between these two peptides (37% heterogeneity) their general structural organization is very similar as shown by their clearly related circular dichroism spectra. Furthermore, Bs6 is a minor component, composed of 38 residues (4.1 kDa) containing six half-cystine residues and having close sequence identities (40-80%) with charybdotoxin-like SCNs containing three disulfide bridges. The non-cysteinic, bacic and thermolabile Bs10 is composed of 34 amino acid residues (3.7 kDa), and belongs to a new class of peptides, with no sequence resemblance to any other so far reported sequence isolated from scorpions. Surprisingly, Bs10 shows some limited sequence analogy with oocyte zinc finger proteins. Results of these studies are discussed with respect to their structural similarities within the scorpion LCNs, SCNs and other biologically active peptides.

Original languageEnglish (US)
Pages (from-to)323-332
Number of pages10
JournalComparative Biochemistry and Physiology - A Molecular and Integrative Physiology
Volume121
Issue number4
DOIs
StatePublished - Dec 1998
Externally publishedYes

Fingerprint

Scorpions
Venoms
Molecular mass
Molecular Structure
Purification
Peptides
Neurotoxins
Disulfides
Cysteine
Charybdotoxin
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Zinc Fingers
Sequence Homology
Circular Dichroism
Ionization
Oocytes
Mass spectrometry
Zinc
Desorption
Molecular Weight

Keywords

  • Biologically active peptides
  • Buthus sindicus
  • Ion channels
  • Primary structure
  • Scorpion
  • Sequence homology
  • Short-chain neurotoxins
  • Venom

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Physiology

Cite this

Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom. / Ali, Syed Abid; Stoeva, Stanka; Schütz, Jürgen; Kayed, Rakez; Abassi, Atiya; Zaidi, Zafar H.; Voelter, Wolfgang.

In: Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology, Vol. 121, No. 4, 12.1998, p. 323-332.

Research output: Contribution to journalArticle

Ali, Syed Abid ; Stoeva, Stanka ; Schütz, Jürgen ; Kayed, Rakez ; Abassi, Atiya ; Zaidi, Zafar H. ; Voelter, Wolfgang. / Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom. In: Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology. 1998 ; Vol. 121, No. 4. pp. 323-332.
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AU - Zaidi, Zafar H.

AU - Voelter, Wolfgang

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AB - The primary structures of four low molecular mass peptides (Bs 6, 8, 10 and 14) from scorpion Buthus sindicus were elucidated via combination of Edman degradation and matrix-assisted laser desorption ionization mass spectrometry. Bs 8 and 14 are cysteine-rich, thermostable peptides composed of 35-36 residues with molecular weights of 3.7 and 3.4 kDa, respectively. These peptides show close sequence homologies (55-78%) with other scorpion chlorotoxin-like short-chain neurotoxins (SCNs) containing four intramolecular disulfide bridges. Despite the sequence variation between these two peptides (37% heterogeneity) their general structural organization is very similar as shown by their clearly related circular dichroism spectra. Furthermore, Bs6 is a minor component, composed of 38 residues (4.1 kDa) containing six half-cystine residues and having close sequence identities (40-80%) with charybdotoxin-like SCNs containing three disulfide bridges. The non-cysteinic, bacic and thermolabile Bs10 is composed of 34 amino acid residues (3.7 kDa), and belongs to a new class of peptides, with no sequence resemblance to any other so far reported sequence isolated from scorpions. Surprisingly, Bs10 shows some limited sequence analogy with oocyte zinc finger proteins. Results of these studies are discussed with respect to their structural similarities within the scorpion LCNs, SCNs and other biologically active peptides.

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