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Toxins 2015, 7(2), 219-237; doi:10.3390/toxins7020219

AaeAP1 and AaeAP2: Novel Antimicrobial Peptides from the Venom of the Scorpion, Androctonus aeneas: Structural Characterisation, Molecular Cloning of Biosynthetic Precursor-Encoding cDNAs and Engineering of Analogues with Enhanced Antimicrobial and Anticancer Activities

1,2,†
,
1,2,†
,
2
,
2,3,* , 2,4
,
1,2,* , 2,* , 2,4
,
1
,
2
and
2
1
School of Pharmaceutical Sciences, China Medical University, Shenyang 110001, China
2
Natural Drug Discovery Group, School of Pharmacy, Queen's University, Belfast BT9 7BL, Northern Ireland, UK
3
Department of Emergency Medicine, the First Hospital of Hebei Medical University, Shijiazhuang 050031, China
4
Jiangsu Key Laboratory for Traditional Chinese Medicine (TCM) Formulae Research, Nanjing University of Chinese Medicine, Nanjing 210023, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Richard J. Lewis
Received: 6 December 2014 / Accepted: 19 January 2015 / Published: 23 January 2015
(This article belongs to the Section Animal Venoms)
View Full-Text   |   Download PDF [876 KB, uploaded 23 January 2015]   |  

Abstract

The main functions of the abundant polypeptide toxins present in scorpion venoms are the debilitation of arthropod prey or defence against predators. These effects are achieved mainly through the blocking of an array of ion channel types within the membranes of excitable cells. However, while these ion channel-blocking toxins are tightly-folded by multiple disulphide bridges between cysteine residues, there are additional groups of peptides in the venoms that are devoid of cysteine residues. These non-disulphide bridged peptides are the subject of much research interest, and among these are peptides that exhibit antimicrobial activity. Here, we describe two novel non-disulphide-bridged antimicrobial peptides that are present in the venom of the North African scorpion, Androctonus aeneas. The cDNAs encoding the biosynthetic precursors of both peptides were cloned from a venom-derived cDNA library using 3'- and 5'-RACE strategies. Both translated precursors contained open-reading frames of 74 amino acid residues, each encoding one copy of a putative novel nonadecapeptide, whose primary structures were FLFSLIPSVIAGLVSAIRN and FLFSLIPSAIAGLVSAIRN, respectively. Both peptides were C-terminally amidated. Synthetic versions of each natural peptide displayed broad-spectrum antimicrobial activities, but were devoid of antiproliferative activity against human cancer cell lines. However, synthetic analogues of each peptide, engineered for enhanced cationicity and amphipathicity, exhibited increases in antimicrobial potency and acquired antiproliferative activity against a range of human cancer cell lines. These data clearly illustrate the potential that natural peptide templates provide towards the design of synthetic analogues for therapeutic exploitation. View Full-Text
Keywords: scorpion; venom; antimicrobial peptide; molecular cloning scorpion; venom; antimicrobial peptide; molecular cloning
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

Du, Q.; Hou, X.; Wang, L.; Zhang, Y.; Xi, X.; Wang, H.; Zhou, M.; Duan, J.; Wei, M.; Chen, T.; Shaw, C. AaeAP1 and AaeAP2: Novel Antimicrobial Peptides from the Venom of the Scorpion, Androctonus aeneas: Structural Characterisation, Molecular Cloning of Biosynthetic Precursor-Encoding cDNAs and Engineering of Analogues with Enhanced Antimicrobial and Anticancer Activities. Toxins 2015, 7, 219-237.

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