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Toxins 2016, 8(2), 36; doi:10.3390/toxins8020036

Structure-Activity Relationship of Chlorotoxin-Like Peptides

1
International Center for Chemical and Biochemical Sciences (ICCBS), HEJ Research Institute of Chemistry, University of Karachi, Karachi-75270, Pakistan
2
Interfaculty Institute of Biochemistry (IIB), University of Tuebingen, Hoppe-Seyler Str. 4, Tuebingen D-72076, Germany
3
Venom Evolution Laboratory, School of Biological Sciences, University of Queensland, Brisbane, QLD 4072, Australia
Present address: Dow International Medical College, Dow University of Health Sciences, Karachi-75270, Pakistan
*
Author to whom correspondence should be addressed.
Academic Editors: Rong Chen and Yingliang Wu
Received: 2 November 2015 / Revised: 18 January 2016 / Accepted: 19 January 2016 / Published: 2 February 2016
(This article belongs to the Special Issue Animal Toxins and Biological Ion Channels)
View Full-Text   |   Download PDF [2792 KB, uploaded 2 February 2016]   |  

Abstract

Animal venom (e.g., scorpion) is a rich source of various protein and peptide toxins with diverse physio-/pharmaco-logical activities, which generally exert their action via target-specific modulation of different ion channel functions. Scorpion venoms are among the most widely-known source of peptidyl neurotoxins used for callipering different ion channels, such as; Na+, K+, Ca+, Cl, etc. A new peptide of the chlorotoxin family (i.e., Bs-Tx7) has been isolated, sequenced and synthesized from scorpion Buthus sindicus (family Buthidae) venom. This peptide demonstrates 66% with chlorotoxin (ClTx) and 82% with CFTR channel inhibitor (GaTx1) sequence identities reported from Leiurus quinquestriatus hebraeus venom. The toxin has a molecular mass of 3821 Da and possesses four intra-chain disulphide bonds. Amino acid sequence analysis of Bs-Tx7 revealed the presence of a scissile peptide bond (i.e., Gly-Ile) for human MMP2, whose activity is increased in the case of tumour malignancy. The effect of hMMP2 on Bs-Tx7, or vice versa, observed using the FRET peptide substrate with methoxycoumarin (Mca)/dinitrophenyl (Dnp) as fluorophore/quencher, designed and synthesized to obtain the lowest Km value for this substrate, showed approximately a 60% increase in the activity of hMMP2 upon incubation of Bs-Tx7 with the enzyme at a micromolar concentration (4 µM), indicating the importance of this toxin in diseases associated with decreased MMP2 activity. View Full-Text
Keywords: CFTR; chlorotoxin; chloride channel; MMP2; peptidyl-inhibitors; scorpion venom CFTR; chlorotoxin; chloride channel; MMP2; peptidyl-inhibitors; scorpion venom
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Ali, S.A.; Alam, M.; Abbasi, A.; Undheim, E.A.B.; Fry, B.G.; Kalbacher, H.; Voelter, W. Structure-Activity Relationship of Chlorotoxin-Like Peptides. Toxins 2016, 8, 36.

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