Antifungal peptide

Marine sponge - Theonella Cyclollthlstide A - antifungal peptide 14, 32... 

Halicylindramides - antifungal peptides Polydiscamide A - cytotoxic peptides... 

HO-./ T V-NH Blue-green algae -Anabaena laxa Marine sponge -Callyspongia abnormis Laxaphycins A and E -antifungal peptides Callynormine A - no bioactivity has been reported 246-248 249... 

Liu, Z., Zeng, M., Dong, S., Xu, J., Song, H., and Zhao, Y. (2007). Effect of an antifungal peptide from oyster enzymatic hydrolysates for control of gray mold (Botrytis cinerea) on harvested strawberries. Postharvest Biol. Technol. 46, 95-98. 

Hyrlios sp. [310,311], and the antifungal peptides halicylindramides from Halicondria sp. [312],... 

Li H, Matsunaga S, Fusetani N (1996) Halicylindramides D and E, Antifungal Peptides from the Marine Sponge Halichondria cylindrata. J Nat Prod 59 163... 

J. A. Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides. /. Biol. Chem. 1994, 269, 33159-33163... 

ANAFP (a novel antifungal peptide) 483 Anakinra 17, 464, 1118 Analytical assay validation... 

In 1989, Fusetani group reported the isolation and the complete structure of theonellamide F (35), a novel antifungal peptide, from a... 

Peschen D, Li H P, Fischer R, et al. (2004). Fusion proteins comprising a Fusarium-specific antibody linked to antifungal peptides protect plants against a fungal pathogen. Nature Biotechnol. 22 732-738. 

Cepacidines, glycopeptides produced by Burkholderia cepacia. Cepacidines Ai and Aj belong to the class of antifungal peptides derived from bacteria and fungi. Both peptides display potent antifungal activity for Candida and other species [C. H. Lee et al., J. Antibiot. 1994, 47, 1402]. 

Gallinacins, a group of mammalian antifungal peptides. They contain three intramolecular disulfide bonds, are relatively cationic, and are rich in Lys and Arg. It has been reported that gallinadn-l and -la inhibit C. albicans in a radial diffusion assay, whereas gallinacin-2 was not active at up to 400 /xg mL in this assay [M. K. Harwig et al, FEBS Lett. 1994, 342, 281]. 

Iturins, a family of antifungal peptides produced by various strains of Bacillus suh-tilis. The iturins comprise small cyclic pep-tidolipids characterized by a lipid-soluble -amino acid linked to a peptide containing D- and L-amino acids [F. Peypoux et al.. Tetrahedron 1973, 29, 3455 M. Klich et al., Mycopathology 1991, 226, 77]. 

Lipid transfer proteins, a family of homologous antifungal peptides containing eight disulfide-linked cysteines produced by some plants. For example, onion seeds (Allium cepa. L) produce the lipid transfer peptide ACE-AMPi, which inhibited F. oxysporum [B. P. A. Cammune et al.. Plant Pathol. 1996, 109, 445]. 

Lunatusin, an antifungal peptide (Mr 7 kDa) isolated from the seeds of Chinese lima bean [Phaseolus lunatus L.). The trypsin-stable peptide exerted an antifungal activity towards various fungal species, and also inhibited proliferation in the breast cancer cell line MCF-7 [J. H. Wong, T. B. Ng, Peptides 2005, 26, 2086]. 

Plant defensins, antifungal peptides which are not related to mammalian or insect defensins. The plant cc-defensins are present in seeds or leaves and are characterized by complex structures. They contain disulfide-linked cysteines in a triple-stranded antiparallel /3-sheet with only one cf-helix, and are homologous to those produced in human and rabbit neutrophils. Plant Q -defensins are not capable of forming ion-permeable pores in artificial membranes, but they may act through a receptor-mediated mechanism. They are considered PR proteins and are classified as members of the PR-12 group [K. Thevissen et al., J. Biol. Chem. 1996, 271,15018 A. J. De Lucca etal.. Can.]. Microbiol. 2005, 51,1001]. 

Comparisons have been made of the 3D structure of hevein in solution with the structures reported for other hevein domains, including WGA and hevein itself in the solid state.Despite differences in the number and nature of several amino acid residues, the polypeptide conformation has also been compared with the NMR-derived structure of a smaller antifungal peptide (30 amino acids) termed Ac-AMP2. The interactions just described have also been observed in the crystal structures of WGA-chitobiose and WGA-sialyllactose (see later). In all cases, the obtained conformations and intermolecular protein-sugar interactions are indeed similar (see later), regardless of the experimental method used to determine the 3D structure. 

Other domains having a five-disulfide motif have also been purified. Two antifungal peptides, named EAFPl and EAFP2, have been isolated from the bark of Eucommia ulmoides Oliv. Each of the sequences consists of 41 residues... 

R. H. Huang, Y. Xiang, G. Z. Tu, Y. Zhang, and D. C. Wang, Solution structure of Eucommia antifungal peptide A novel structural model distinct with a five-disulfide motif. Biochemistry, 43 (2004) 6005-6012. 

H. Hemmi, J. Ishibashi, T. Tomie, and M. Yamakawa, Structural basis for new pattern of conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle Oryctes rhinoceros, J. Biol. Chem., 278 (2003) 22820-22827. 

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