Abstract
Most spider antimicrobial peptides share a common mechanism of membrane permeabilisation and the innate immune systems of the pathogen. In this review, we present recent accounts of the application at the preclinical level that should be tried and the range of bioactivities and their particular structure can be harnessed for molecular engineering applications and in drug design. Structural analyses such as amino acid sequence and circular dichroism are described. Conductance measurements and pharmacological studies of the action on the inner or outer membranes of anti-microbe will reveal more about the mode of action of the antimicrobial peptides of spider.
Keywords: venoms, neurotoxins, antimicrobial peptides, lycosa singoriensis, lycotoxin, tachystatin a, oxyopinin, gomesin
Protein & Peptide Letters
Title: Pharmacological Characterisation of Spider Antimicrobial Peptides
Volume: 12 Issue: 6
Author(s): Li Gao, Jing Zhang, Wei Feng, Na Bao, Daxiang Song and Bao-Cheng Zhu
Affiliation:
Keywords: venoms, neurotoxins, antimicrobial peptides, lycosa singoriensis, lycotoxin, tachystatin a, oxyopinin, gomesin
Abstract: Most spider antimicrobial peptides share a common mechanism of membrane permeabilisation and the innate immune systems of the pathogen. In this review, we present recent accounts of the application at the preclinical level that should be tried and the range of bioactivities and their particular structure can be harnessed for molecular engineering applications and in drug design. Structural analyses such as amino acid sequence and circular dichroism are described. Conductance measurements and pharmacological studies of the action on the inner or outer membranes of anti-microbe will reveal more about the mode of action of the antimicrobial peptides of spider.
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Cite this article as:
Gao Li, Zhang Jing, Feng Wei, Bao Na, Song Daxiang and Zhu Bao-Cheng, Pharmacological Characterisation of Spider Antimicrobial Peptides, Protein & Peptide Letters 2005; 12 (6) . https://dx.doi.org/10.2174/0929866054395806
DOI https://dx.doi.org/10.2174/0929866054395806 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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