Home » Calcium Binding Protein Modulators » Following peptides sequences are shown in alignment: MBP-1 from (“type”:”entrez-protein”,”attrs”:”text”:”P28794″,”term_id”:”126793″,”term_text”:”P28794″P28794); EcAMP1 from (“type”:”entrez-protein”,”attrs”:”text”:”P86698″,”term_id”:”353678014″,”term_text”:”P86698″P86698); Tk-AMP-X1 (“type”:”entrez-protein”,”attrs”:”text”:”CCP19155

Following peptides sequences are shown in alignment: MBP-1 from (“type”:”entrez-protein”,”attrs”:”text”:”P28794″,”term_id”:”126793″,”term_text”:”P28794″P28794); EcAMP1 from (“type”:”entrez-protein”,”attrs”:”text”:”P86698″,”term_id”:”353678014″,”term_text”:”P86698″P86698); Tk-AMP-X1 (“type”:”entrez-protein”,”attrs”:”text”:”CCP19155

Following peptides sequences are shown in alignment: MBP-1 from (“type”:”entrez-protein”,”attrs”:”text”:”P28794″,”term_id”:”126793″,”term_text”:”P28794″P28794); EcAMP1 from (“type”:”entrez-protein”,”attrs”:”text”:”P86698″,”term_id”:”353678014″,”term_text”:”P86698″P86698); Tk-AMP-X1 (“type”:”entrez-protein”,”attrs”:”text”:”CCP19155.1″,”term_id”:”506209979″,”term_text”:”CCP19155.1″CCP19155.1); Sm-AMP-X (“type”:”entrez-protein”,”attrs”:”text”:”C0HJD6″,”term_id”:”613779808″C0HJD6); Luffin P1 from (“type”:”entrez-protein”,”attrs”:”text”:”P85981″,”term_id”:”206557922″,”term_text”:”P85981″P85981); BWI-2b, and BWI-2c from (no accession number and “type”:”entrez-protein”,”attrs”:”text”:”P86794″,”term_id”:”403399439″,”term_text”:”P86794″P86794); C2 peptide from (“type”:”entrez-protein”,”attrs”:”text”:”Q9ZWI3″,”term_id”:”75217145″,”term_text”:”Q9ZWI3″Q9ZWI3). pathogenic fungi and bacteria (Duvick et al., 1992). TABLE 1 Diversity of -hairpinins from plants. (Poaceae)Duvick et al., 19922MiAMP2c, (“type”:”entrez-protein”,”attrs”:”text”:”Q9SPL5″,”term_id”:”75207036″,”term_text”:”Q9SPL5″Q9SPL5)Antifungal ((Proteaceae)Marcus et al., 1999, 2008MiAMP2b, MiAMP2dAntifungal ((Poaceae)Nolde et al., 2011; Rogozhin et al., 2012, 2018b; Ryazantsev et al., 2014, 2019EcAMP1-HypAntifungal ((Poaceae)Utkina et al., 20136Sm-AMP-X (“type”:”entrez-protein”,”attrs”:”text”:”C0HJD6″,”term_id”:”613779808″C0HJD6)Antifungal HA-100 dihydrochloride ((Caryophyllaceae)Slavokhotova et al., 2014bSm-AMP-L, Sm-AMP-X1, Sm-AMP-X2Antifungal ((Plantaginaceae)Conners et al., 20078BWI-2a BWI-2b BWI-2c (“type”:”entrez-protein”,”attrs”:”text”:”P86794″,”term_id”:”403399439″,”term_text”:”P86794″P86794)Trypsin inhibitor(Polygonaceae)Park et al., 1997; Oparin et al., 20129FtAMPTrypsin inhibitor, antifungal (sp., and sp., and (Polygonaceae)Cui et al., 201810C2 (“type”:”entrez-protein”,”attrs”:”text”:”Q9ZWI3″,”term_id”:”75217145″,”term_text”:”Q9ZWI3″Q9ZWI3)Trypsin inhibitor(Cucurbitaceae)Yamada et al., 19996.5k-AGRP, Luffin P1 (“type”:”entrez-protein”,”attrs”:”text”:”P56568″,”term_id”:”3912993″,”term_text”:”P56568″P56568)Ribosome-inactivating(Cucurbitaceae)Kimura et al., 1997; Li et al., 2003 Open in a separate window Open in a separate windows FIGURE 1 Amino acid sequence alignment of -hairpinin peptides. Following peptides sequences are shown in alignment: MBP-1 from (“type”:”entrez-protein”,”attrs”:”text”:”P28794″,”term_id”:”126793″,”term_text”:”P28794″P28794); EcAMP1 from (“type”:”entrez-protein”,”attrs”:”text”:”P86698″,”term_id”:”353678014″,”term_text”:”P86698″P86698); Tk-AMP-X1 (“type”:”entrez-protein”,”attrs”:”text”:”CCP19155.1″,”term_id”:”506209979″,”term_text”:”CCP19155.1″CCP19155.1); Sm-AMP-X (“type”:”entrez-protein”,”attrs”:”text”:”C0HJD6″,”term_id”:”613779808″C0HJD6); Luffin P1 from (“type”:”entrez-protein”,”attrs”:”text”:”P85981″,”term_id”:”206557922″,”term_text”:”P85981″P85981); BWI-2b, and BWI-2c from (no accession number and “type”:”entrez-protein”,”attrs”:”text”:”P86794″,”term_id”:”403399439″,”term_text”:”P86794″P86794); C2 peptide from (“type”:”entrez-protein”,”attrs”:”text”:”Q9ZWI3″,”term_id”:”75217145″,”term_text”:”Q9ZWI3″Q9ZWI3). The cysteine residues are shown in gray; disulfide bridges shown in black lines above; the functional for trypsin inhibitors Arg HA-100 dihydrochloride residues are boxed. Marcus et al. (1999) found an antifungal -hairpinin in (Marcus et al., 1999). The peptide named MiAMP2c was purified HA-100 dihydrochloride from nut kernels (genus (with EC50 ranging from 1 to 10 M. The observed activity was comparable to that of MBP-1: the effective concentrations of both peptides against were around 4 M. By light microscope assay, it was revealed that EcAMP1 prevented hyphae elongation without cytoplasmic membrane lysis. Moreover, experiments with species showed that this peptide did not impact the germination from your conidia itself (Nolde et al., 2011). Accordingly, this was the first plant -hairpinin demonstrated to have fungistatic activity. The mechanism of action of EcAMP1 against was further investigated with a combination of classical microbiological approaches and various microscopy techniques (Vasilchenko et al., 2016). Optical microscopy observation revealed a linear correlation between the dose and the response at a concentration of EcAMP1 less than the Rabbit Polyclonal to Histone H2A IC50. The antimicrobial effect was more pronounced against germinated conidia than against the ungerminated stage. Using high-resolution laser scanning fluorescence microscopy, an conversation between EcAMP1 and the target HA-100 dihydrochloride cell was observed. At the first stage, the active peptide bound with components of the fungal cell wall (with glycans, glycoproteins, and proteins-amyloids) and distributed uniformly over the entire cellular surface. At the second stage, the peptide expanded in the cell barrier structures uniformly, presumably due to an abundance of binding sites located homogeneously across the plasma membrane and/or cell walls of the conidia surface. Moreover, if the concentration of EcAMP1 was greater than IC50, the roughness of the conidia surface increased, and the cell volume decreased in a dose-dependent manner. Perhaps the most plausible mechanism of EcAMP1 action is an induction of apoptosis, leading to fungal programmed cell death, different to the membrane-disruption mechanisms of action of various other herb AMPs (Vasilchenko et al., 2016). Besides EcAMP1, several peptides with specific -hairpinin Cys-motifs were purified from barnyard grass (and reduced binding affinity with commercial polysaccharides, chitin, and -1.3-glucan (Rogozhin et al., 2018a). EcAMP2 and its truncated analog EcAMP2.1 contained 31 and 26 aa residues, respectively, and were slightly homologous to EcAMP1 (approximately 40% similarity between EcAMP1 and EcAMP2) (Rogozhin et al., 2012). These two peptides equally decreased the growth of zoosporangia of at a concentration of 24 M, were not able to inhibit colony growth of any bacterial species tested, and experienced no trypsin-inhibitory activity (Rogozhin et al., 2012). EcAMP3 has 35 aa residues and shares 40% homology to the EcAMP1 peptide (Ryazantsev et al., 2014). This peptide showed no trypsin inhibitory activity but experienced a significant inhibitory effect on mycelium growth of some phytopathogenic fungi (Table 1). Unlike EcAMP1 and EcAMP2, EcAMP3 suppressed the growth of bacteria with an IC50 ranging between 10 M (at a concentration of 8 M, while EcAMP4.1 was less effective and had an IC50 that ranged between 12 and 18 M. The authors concluded that among all analyzed EcAMPs, the EcAMP1, EcAMP3, and EcAMP4 peptides have similar activities, peptide EcAMP4.1 was less active, and peptides Ec-AMP2 and EcAMP2.1 were almost inactive (Ryazantsev et al., 2019). Two -hairpinins were isolated from seeds of wheat and named Tk-AMP-X1 and Tk-AMP-X2 (Utkina et al., 2013). These highly comparable molecules contained 31 and 28 aa, respectively, as well as the -hairpinins Cys-motif. at equivalent concentrations (IC50 = 7.5 M), but were less active against (IC50 ranged from 10 to 15 M), and experienced relatively high concentrations against (IC50 between 17 and 30 M). Neither of the wheat peptides exhibits protease inhibitory activity.