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Antifungal Peptides (antifungal + peptide)
Selected AbstractsPurification of Angularin, A Novel Antifungal Peptide from Adzuki BeansJOURNAL OF PEPTIDE SCIENCE, Issue 3 2002Dr X. Y. Ye Abstract An antifungal peptide was isolated from the adzuki bean with a procedure involving affinity chromatography on Affi-gel blue gel and ion exchange chromatography on CM-Sepharose. The protein designated angularin was adsorbed on both types of chromatographic media and possessed a molecular weight of 8 kDa. Angularin exhibited antifungal activity against a variety of fungal species including Mycospharella arachidiocola and Botrytis cinerea. It inhibited mycelial growth in B. cinerea with an IC50 of 14.3 µM. Fusarium oxysporum and Rhizoctonia solani were not inhibited. Angularin demonstrated inhibitory activity on translation in the rabbit reticulocyte lysate system (IC50 = 8.0 µM) but did not affect proliferation of splenocytes. The activity of HIV-1 reverse transcriptase was inhibited in the presence of angularin. Its N -terminal sequence was GEPGQKE. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd. [source] Lipid transfer proteins from Brassica campestris and mung bean surpass mung bean chitinase in exploitabilityJOURNAL OF PEPTIDE SCIENCE, Issue 10 2007Peng Lin Abstract Antifungal peptides with a molecular mass of 9 kDa and an N -terminal sequence demonstrating remarkable similarity to those of nonspecific lipid transfer proteins (nsLTPs) were isolated from seeds of the vegetable Brassica campestris and the mung bean. The purified peptides exerted an inhibitory action on mycelial growth in various fungal species. The antifungal activity of Brassica and mung bean nsLTPs were thermostable, pH-stable, and stable after treatment with pepsin and trypsin. In contrast, the antifungal activity of mung bean chitinase was much less stable to changes in pH and temperature. Brassica LTP inhibited proliferation of hepatoma Hep G2 cells and breast cancer MCF 7 cells with an IC50 of 5.8 and 1.6 µM, respectively, and the activity of HIV-1 reverse transcriptase with an IC50 of 4 µM. However, mung bean LTP and chitinase were devoid of antiproliferative and HIV-1 reverse transcriptase inhibitory activities. In contrast to the mung bean LTP, which exhibited antibacterial activity, Brassica LTP was inactive. All three antifungal peptides lacked mitogenic activity toward splenocytes. These results indicate that the two LTPs have more desirable activities than the chitinase and that there is a dissociation between the antifungal and other activities of these antifungal proteins. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd. [source] Purification of Angularin, A Novel Antifungal Peptide from Adzuki BeansJOURNAL OF PEPTIDE SCIENCE, Issue 3 2002Dr X. Y. Ye Abstract An antifungal peptide was isolated from the adzuki bean with a procedure involving affinity chromatography on Affi-gel blue gel and ion exchange chromatography on CM-Sepharose. The protein designated angularin was adsorbed on both types of chromatographic media and possessed a molecular weight of 8 kDa. Angularin exhibited antifungal activity against a variety of fungal species including Mycospharella arachidiocola and Botrytis cinerea. It inhibited mycelial growth in B. cinerea with an IC50 of 14.3 µM. Fusarium oxysporum and Rhizoctonia solani were not inhibited. Angularin demonstrated inhibitory activity on translation in the rabbit reticulocyte lysate system (IC50 = 8.0 µM) but did not affect proliferation of splenocytes. The activity of HIV-1 reverse transcriptase was inhibited in the presence of angularin. Its N -terminal sequence was GEPGQKE. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd. [source] Lipid transfer proteins from Brassica campestris and mung bean surpass mung bean chitinase in exploitabilityJOURNAL OF PEPTIDE SCIENCE, Issue 10 2007Peng Lin Abstract Antifungal peptides with a molecular mass of 9 kDa and an N -terminal sequence demonstrating remarkable similarity to those of nonspecific lipid transfer proteins (nsLTPs) were isolated from seeds of the vegetable Brassica campestris and the mung bean. The purified peptides exerted an inhibitory action on mycelial growth in various fungal species. The antifungal activity of Brassica and mung bean nsLTPs were thermostable, pH-stable, and stable after treatment with pepsin and trypsin. In contrast, the antifungal activity of mung bean chitinase was much less stable to changes in pH and temperature. Brassica LTP inhibited proliferation of hepatoma Hep G2 cells and breast cancer MCF 7 cells with an IC50 of 5.8 and 1.6 µM, respectively, and the activity of HIV-1 reverse transcriptase with an IC50 of 4 µM. However, mung bean LTP and chitinase were devoid of antiproliferative and HIV-1 reverse transcriptase inhibitory activities. In contrast to the mung bean LTP, which exhibited antibacterial activity, Brassica LTP was inactive. All three antifungal peptides lacked mitogenic activity toward splenocytes. These results indicate that the two LTPs have more desirable activities than the chitinase and that there is a dissociation between the antifungal and other activities of these antifungal proteins. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd. [source] Investigation of relationships between barley stress peptides and beer gushing using SDS-PAGE and MS screeningJOURNAL OF SEPARATION SCIENCE, JSS, Issue 23-24 2009Blanka Hégrová Abstract The relationship between gushing and antifungal peptides in barley and malt kernels was examined for five barley varieties produced in the Czech Republic with four conditions of infection and treatment. Proteome changes during pathogen-seed interaction were observed with SDS-PAGE and MALDI-TOF MS. These methods were applied as a fast screening for observing the relationship between gushing and peptides/proteins. It was found that the presence of basic peptides, presumably hordothionins and non-specific lipid transfer protein type 1, did not correlate with the degree of gushing for malt (,r,,<0.07, 0.34>), (,r,,<0.01, 0.49>), respectively, as detected by both methods. [source] Primary structural determination of N-terminally blocked peptides from the bark of Eucommia ulmoides Oliv by mass spectrometric analysisRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 9 2003Ren-Huai Huang Sequencing of N-terminally blocked proteins/peptides is a challenge since these molecules inhibit processing by Edman degradation. By using high accuracy Fourier transform ion cyclotron resonance (FTICR) tandem mass spectrometry and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS), the primary structures of two novel N-terminally blocked antifungal peptides (EAFP1 and EAFP2), purified from the bark of Eucommia ulmoides Oliv, have been determined. The results show that the high mass accuracy provided by FTICR mass spectrometry is effective to determine the N-terminally blocking group, and can simplify the task of spectral interpretation and improve the precision of sequence determination. The combination of MALDI-TOFMS with carboxyl peptidase Y digestion was used to determine the C-terminal 36- and 27-residue sequences of EAFP1 and EAFP2, respectively, to provide the sequence linkage information for tryptic fragments. Compared with traditional peptide chemistry the advantage of mass spectrometric techniques is their simplicity, speed and sensitivity. Copyright © 2003 John Wiley & Sons, Ltd. [source] Crystallization and preliminary crystallographic studies of a novel antifungal protein with five disulfide bridges from Eucommia ulmoides OliverACTA CRYSTALLOGRAPHICA SECTION D, Issue 10-2 2002Ye Xiang Two antifungal proteins, named Eucommia antifungal peptides 1 and 2 (EAFP1 and EAFP2), have been purified from the bark of the tree E. ulmoides Oliver and show a relatively broad spectrum of antifungal activity against several agriculturally important plant pathogens. One of these small proteins (EAFP2) has been crystallized. The crystal belongs to space group P21, with unit-cell parameters a = 19.01, b = 23.16, c = 30.69,Å, , = 98.54°. 1.0,Å resolution data were collected from an EAFP2 crystal and have been used to obtain phase information directly by an ab initio method. [source] | ||||||||||