27.01.2013 Views

Molecular Characterization and Gene Expression Profiling ... - CUSAT

Molecular Characterization and Gene Expression Profiling ... - CUSAT

Molecular Characterization and Gene Expression Profiling ... - CUSAT

SHOW MORE
SHOW LESS

Create successful ePaper yourself

Turn your PDF publications into a flip-book with our unique Google optimized e-Paper software.

Chapter 1<br />

quite opposite characteristics with respect to antibacterial activity. Indeed,<br />

different peptides may be membrane permeabilizing at their minimal<br />

effective concentrations or at concentrations well above or well below these<br />

concentrations. Nonetheless, antibacterial peptides seem largely able to affect<br />

their antimicrobial activity because of their amphipathicity or amphiphilicity<br />

<strong>and</strong> because of the presence of regions within the folded structure with high<br />

concentrations of positively charged residues (Powers et al., 2004).<br />

Mechanism of antibacterial activity<br />

As described in section 1.1.3.9.<br />

1.7.10.7 Antifungal peptides<br />

Knowledge of antifungal peptides has accelerated in recent years.<br />

Their mode of action was first described as involving either fungal cell lysis<br />

or interference with fungal cell wall synthesis (de Lucca <strong>and</strong> Walsh, 1999).<br />

However, as the numbers of known antifungal peptides increase, new modes<br />

of action are being identified. It is intriguing to note that peptides with<br />

primarily antifungal activity, such as many of those isolated from plants,<br />

tend to be relatively rich in polar <strong>and</strong> neutral amino acids, suggesting a<br />

unique structure-activity relationship (Lustig et al., 1996).<br />

Structural requirements for antifungal peptides<br />

Studies have shown that antifungal peptides vary substantially in<br />

sequence <strong>and</strong> structure, <strong>and</strong> peptides as structurally diverse as eucommia<br />

(Huang et al., 2004), the α-helical P18 (Lee et al., 2004), <strong>and</strong> the extended<br />

peptide indolicidin (Lee et al., 2003), as well as plant defensins <strong>and</strong> a<br />

coleopteran β-sheet peptide from Acrocinus longimanus (Barbault et al., 2003),<br />

have all shown antifungal activity. Thus, like for antibacterial peptides, there<br />

are no obvious conserved structural domains that give rise to antifungal<br />

activity. Modification of ineffective AMPs has revealed that relatively<br />

modest changes often result in antifungal activity. Although no conserved<br />

sequences are evident for the antifungal peptides, several have been<br />

<strong>Molecular</strong> <strong>Characterization</strong> <strong>and</strong> <strong>Gene</strong> <strong>Expression</strong> <strong>Profiling</strong> of Antimicrobial Peptides in Penaeid Shrimps<br />

73

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!