scholarly journals Amino Acid Sequence and Antimicrobial Activity of Chitin-Binding Peptides,Pp-AMP 1 andPp-AMP 2, from Japanese Bamboo Shoots (Phyllostachys pubescens)

2005 ◽  
Vol 69 (3) ◽  
pp. 642-645 ◽  
Author(s):  
Masatoshi FUJIMURA ◽  
Mineo IDEGUCHI ◽  
Yuji MINAMI ◽  
Keiichi WATANABE ◽  
Kenjiro TADERA
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phyllostachys Pubescens ◽  
Bamboo Shoots ◽  
Binding Peptides

scholarly journals Cloning and Expression of Synthetic Genes Encoding the Broad Antimicrobial Spectrum Bacteriocins SRCAM 602, OR-7, E-760, and L-1077, by RecombinantPichia pastoris

2015 ◽  
Vol 2015 ◽  
pp. 1-11 ◽  
Author(s):  
Sara Arbulu ◽  
Juan J. Jiménez ◽  
Loreto Gútiez ◽  
Luis M. Cintas ◽  
Carmen Herranz ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Hydrophobic Interaction ◽  
Peptide Fragments ◽  
Antimicrobial Spectrum ◽  
Synthetic Genes ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Tof Ms

We have evaluated the cloning and functional expression of previously described broad antimicrobial spectrum bacteriocins SRCAM 602, OR-7, E-760, and L-1077, by recombinantPichia pastoris. Synthetic genes, matching the codon usage ofP. pastoris, were designed from the known mature amino acid sequence of these bacteriocins and cloned into the protein expression vector pPICZαA. The recombinant derived plasmids were linearized and transformed into competentP. pastorisX-33, and the presence of integrated plasmids into the transformed cells was confirmed by PCR and sequencing of the inserts. The antimicrobial activity, expected in supernatants of the recombinantP. pastorisproducers, was purified using a multistep chromatographic procedure including ammonium sulfate precipitation, desalting by gel filtration, cation exchange-, hydrophobic interaction-, and reverse phase-chromatography (RP-FPLC). However, a measurable antimicrobial activity was only detected after the hydrophobic interaction and RP-FPLC steps of the purified supernatants. MALDI-TOF MS analysis of the antimicrobial fractions eluted from RP-FPLC revealed the existence of peptide fragments of lower and higher molecular mass than expected. MALDI-TOF/TOF MS analysis of selected peptides from eluted RP-FPLC samples with antimicrobial activity indicated the presence of peptide fragments not related to the amino acid sequence of the cloned bacteriocins.

The Topology of the Plastoquinone and Herbicide Binding Peptides of Photosystem II in the Thylakoid Membrane

1986 ◽  
Vol 41 (1-2) ◽  
pp. 240-246 ◽  
Author(s):  
Achim Trebst
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Amino Acid Sequence ◽  
Thylakoid Membrane ◽  
Higher Plants ◽  
Binding Peptide ◽  
X Ray ◽  
Hydropathy Index ◽  
Herbicide Binding ◽  
Binding Peptides

Abstract The 32 kDa herbicide and QB binding peptide (D-1 protein) and its homologous 34 kDa peptide (D-2 protein) are integral membrane subunits of photosystem II. A model for their folding through the thylakoid membrane in five transmembrane a-helices is proposed from the compari­son of amino acid sequence and hydropathy index plot homologies with subunits of the bacterial system. Following recent data on the X-ray structure of a bacterial photosystem the binding niche for QB is interpreted on the basis of the amino acid changes found in the 32 kDa peptide in herbicide tolerant higher plants and algae.

scholarly journals Identification and Characterization of a Hexapeptide with Activity Against Phytopathogenic Fungi That Cause Postharvest Decay in Fruits

2000 ◽  
Vol 13 (8) ◽  
pp. 837-846 ◽  
Author(s):  
Belén López-García ◽  
Luis González-Candelas ◽  
Enrique Pérez-Payá ◽  
Jose F. Marcos
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Plant Protection ◽  
Phytopathogenic Fungi ◽  
Bacterial Strains ◽  
General Sequence ◽  
Postharvest Decay ◽  
Structure Conservation

A hexapeptide of amino acid sequence Ac-Arg-Lys-Thr-Trp-Phe-Trp-NH 2 was demonstrated to have antimicrobial activity against selected phytopathogenic fungi that cause postharvest decay in fruits. The peptide synthesized with either all D- or all L-amino acids inhibited the in vitro growth of strains of Penicillium italicum, P. digitatum, and Botrytis cinerea, with MICs of 60 to 80 μM and 50% inhibitory concentration (IC50) of 30 to 40 μM. The inhibitory activity of the peptide was both sequence- and fungus-specific since (i) sequence-related peptides lacked activity (including one with five residues identical to the active sequence), (ii) other filamentous fungi (including some that belong to the genus Penicillium) were insensitive to the peptide's antifungal action, and (iii) the peptide did not inhibit the growth of several yeast and bacterial strains assayed. Experiments on P. digitatum identified conidial germination as particularly sensitive to inhibition although mycelial growth was also affected. Our findings suggest that the inhibitory effect is initially driven by the electrostatic interaction of the peptide with fungal components. The antifungal peptide retarded the blue and green mold diseases of citrus fruits and the gray mold of tomato fruits under controlled inoculation conditions, thus providing evidence for the feasibility of using very short peptides in plant protection. This and previous studies with related peptides indicate some degree of peptide amino acid sequence and structure conservation associated with the antimicrobial activity, and suggest a general sequence layout for short antifungal peptides, consisting of one or two positively charged residues combined with aromatic amino acid residues.

An Antimicrobial Peptide from the Australian Native Hardenbergia violacea Provides the First Functionally Characterised Member of a Subfamily of Plant Defensins

1997 ◽  
Vol 24 (5) ◽  
pp. 571 ◽  
Author(s):  
Stuart J. Harrison ◽  
John P. Marcus ◽  
Kenneth C. Goulter ◽  
Jodie L. Green ◽  
Donald J. Maclean ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Antimicrobial Peptide ◽  
Mammalian Cells ◽  
Amino Acid Sequences ◽  
Plant Defensin ◽  
Defensive Role ◽  
Plant Defensins

An antimicrobial peptide (HvAMP1) was isolated from seeds of the Australian native legume Hardenbergia violacea (Schneev.) Stearn. The peptide is 47 amino acid residues in length, contains 8 cysteines, and has a molecular weight of 5392 and a predicted pI of 10.41. HvAMP1 inhibited the growth of several plant pathogenic fungi at concentrations as low as 1 µM in vitro and produced distinct hyphal distortion and increased branching. This antimicrobial activity was greatly diminished in the presence of 1 mM CaCl2 and 50 mM KCl. The purified peptide at 40 µM did not inhibit three different a-amylase enzymes. Aeukaryotic cell-free translation system showed inhibition approaching 50% in the presence of ~100 µM of HvAMP1. The viability of plant and mammalian cells cultured in vitro was not adversely affected by concentrations of HvAMP1 as high as 40 mM. The amino acid sequence of HvAMP1 contained the consensus amino acids that define the plant defensin family of peptides. The HvAMP1 amino acid sequence showed 87% and 57% identity with the amino acid sequences deduced from cDNA sequences from defensins of Vigna unguiculata and Pisum sativum, respectively. Other plant defensin sequences showed less than 33% amino acid identity to the peptide. Therefore, HvAMP1 and the putative plant defensins of cowpea and pea define a distinct sequence subfamily of plant defensins which is at present limited to members of the Fabaceae. HvAMP1 is the first member of this subfamily to be purified and functionally characterised. The antimicrobial activity of HvAMP1 suggests a defensive role for this subfamily of peptides.

scholarly journals Amino Acid Sequences of Lactoferrin from Red Deer (Cervus elaphus) Milk and Antimicrobial Activity of Its Derived Peptides Lactoferricin and Lactoferrampin

Foods ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1305
Author(s):  
Ye Wang ◽  
James D. Morton ◽  
Alaa EL-Din A. Bekhit ◽  
Alan Carne ◽  
Susan L. Mason
Keyword(s):  
Amino Acids ◽  
Antimicrobial Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Positive Charge ◽  
Antimicrobial Activities ◽  
Amino Acid Sequences ◽  
Bovine Lactoferrin ◽  
E Coli ◽  
Net Positive Charge

Although the bioactivities of bovine lactoferrin have been extensively investigated, little is known about deer milk lactoferrin bioactivity and its amino acid sequence. This research investigated the amino acid sequence of deer lactoferrin and the antimicrobial activities of two lactoferrin-encrypted peptides; lactoferricin (Lfcin) and lactoferrampin (Lfampin). Deer lactoferrin was found to have a molecular weight of 77.1 kDa and an isoelectric point of 7.99, which are similar to that of bovine lactoferrin, 78 kDa and pI 7.9. Deer lactoferrin contains 707 amino acids, one amino acid less than bovine lactoferrin, and has 92% homology with bovine lactoferrin. Deer lactoferricin exhibited strong antimicrobial activity against E. coli American Type Culture Collection (ATCC) 25922 and L. acidophilus ATCC 4356. The antimicrobial activities of deer and bovine Lfcin and Lfampin were compared. Based on MIC, deer Lfcin was found to be a more effective inhibitor of L. acidophilus ATCC 4356 than bovine Lfcin, but bovine Lfcin and Lfampin were more effective against E. coli ATCC 25922 than deer Lfcin and Lfampin. The deer Lfcin sequence differed at seven amino acids from bovine Lfcin and this decreased the net positive charge and increased the hydrophobicity. Deer Lfampin contained two differences in amino acid sequence compared to bovine Lfampin which decreased the net positive charge. These amino acid sequence differences likely account for differences in antibacterial activity. Positive charge and hydrophobic residues provide the amphipathic character of these helical peptides, and are considered important for binding of antimicrobial peptides. In silico modelling of deer Lfcin indicated an identical α-helical structure compared to bovine Lfcin.

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

1993 ◽  
Vol 69 (03) ◽  
pp. 217-220 ◽  
Author(s):  
Jonathan B Rosenberg ◽  
Peter J Newman ◽  
Michael W Mosesson ◽  
Marie-Claude Guillin ◽  
David L Amrani
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Point Mutation ◽  
Genomic Dna ◽  
Comparative Sequence Analysis ◽  
Chain Gene ◽  
Molecular Defect ◽  
Nucleotide Position ◽  
Normal Individuals ◽  
Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

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