scholarly journals Pre-structured hydrophobic peptide β-strands: A universal amyloid trap?

2019 ◽  
Vol 664 ◽  
pp. 51-61 ◽  
Author(s):  
Kalkena Sivanesam ◽  
Niels Andersen
Keyword(s):  
Hydrophobic Peptide

Induction of apoptosis in a human lymphoma cell line by hydrophobic peptide fraction separated from anchovy sauce

BioFactors ◽  
2004 ◽  
Vol 21 (1-4) ◽  
pp. 63-67 ◽  
Author(s):  
Young Gon Lee ◽  
Ki Won Lee ◽  
Ji Yeon Kim ◽  
Kyoung Heon Kim ◽  
Hyong Joo Lee
Keyword(s):  
Cell Line ◽  
Lymphoma Cell ◽  
Lymphoma Cell Line ◽  
Peptide Fraction ◽  
Hydrophobic Peptide ◽  
Human Lymphoma ◽  
Anchovy Sauce ◽  
Induction Of Apoptosis

Fabrication of nanoporous material from a hydrophobic peptide

CrystEngComm ◽  
2011 ◽  
Vol 13 (8) ◽  
pp. 3064 ◽  
Author(s):  
Sibaprasad Maity ◽  
Poulami Jana ◽  
Debasish Haldar*
Keyword(s):  
Nanoporous Material ◽  
Hydrophobic Peptide

Hydrophobic peptide interactions with phospholipids

2004 ◽  
Vol 249 (1-3) ◽  
pp. 15-18 ◽  
Author(s):  
F. Reig ◽  
A. Juvé ◽  
P. Sospedra ◽  
L. Rodríguez
Keyword(s):  
Peptide Interactions ◽  
Hydrophobic Peptide

scholarly journals Characteristics and genetic determinant of a hydrophobic peptide bacteriocin, carnobacteriocin A, produced by Carnobacterium piscicola LV17A

Microbiology ◽  
1994 ◽  
Vol 140 (3) ◽  
pp. 517-526 ◽  
Author(s):  
R. W. Worobo ◽  
T. Henkel ◽  
M. Sailer ◽  
K. L. Roy ◽  
J. C. Vederas ◽  
...  
Keyword(s):  
Genetic Determinant ◽  
Carnobacterium Piscicola ◽  
Hydrophobic Peptide

A developmentally regulated membrane protein gene in Dictyostelium discoideum is also induced by heat shock and cold shock

1988 ◽  
Vol 8 (1) ◽  
pp. 153-159
Author(s):  
M Maniak ◽  
W Nellen
Keyword(s):  
Heat Shock ◽  
Membrane Protein ◽  
Rna Processing ◽  
Cold Shock ◽  
Protein Gene ◽  
Nuclear Accumulation ◽  
Control Mechanisms ◽  
Developmentally Regulated ◽  
Hydrophobic Peptide ◽  
Membrane Protein Gene

We have analyzed the expression of the Dictyostelium gene P8A7 which had been isolated as a cDNA clone from an early developmentally regulated gene. The single genomic copy generated two mRNAs which were subject to different control mechanisms: while one mRNA (P8A7S) was regulated like the cell-type-nonspecific late genes, the other one (P8A7L) was induced during development, when cells were allowed to attach to a substrate, and when cells were subjected to stress, such as heat shock and cadmium. Interestingly the same induction was also observed with cold shock. RNA processing was inhibited by heat and cold shock, leading to nuclear accumulation of a precursor. The translated region of the cDNA was common to both mRNAs and encoded an unusually hydrophobic peptide with the characteristics of a membrane protein.

The Structural Gene for Microcin H47 Encodes a Peptide Precursor with Antibiotic Activity

1999 ◽  
Vol 43 (9) ◽  
pp. 2176-2182 ◽  
Author(s):  
Eliana Rodríguez ◽  
Carina Gaggero ◽  
Magela Laviña
Keyword(s):  
Escherichia Coli ◽  
Gene Fusion ◽  
Genetic System ◽  
Antibiotic Activity ◽  
Peptide Antibiotic ◽  
Bifunctional Protein ◽  
Naturally Occurring ◽  
Hydrophobic Peptide ◽  
Peptide Precursor ◽  
Highly Hydrophobic

ABSTRACT Microcin H47 is a bactericidal antibiotic produced by a naturally occurring Escherichia coli strain isolated in Uruguay. The microcin genetic system is located in the chromosome and extends over a 10-kb DNA segment containing the genes required for microcin synthesis, secretion, and immunity. The smallest microcin synthesis gene,mchB, was sequenced and shown to encode a highly hydrophobic peptide. An mchB-phoA gene fusion, which directed the synthesis of a hybrid bifunctional protein with both PhoA and microcin H47-like activities, was isolated. The results presented herein lead us to propose that microcin H47 is indeed a ribosomally synthesized peptide antibiotic and that its peptide precursor already has antibiotic activity of the same specificity as that of mature microcin.

A Novel Approach to Unzipped Tubes Synthesis Using Sulfanilic Acid as the Backbone Amino Acid

2019 ◽  
Vol 57 ◽  
pp. 17-30
Author(s):  
Christopher Narh ◽  
Charles Frimpong ◽  
Qu Fu Wei
Keyword(s):  
Differential Scanning Calorimetry ◽  
Bond Formation ◽  
Sulfanilic Acid ◽  
Test Results ◽  
X Ray Diffraction ◽  
Scanning Calorimetry ◽  
Torsion Angles ◽  
X Ray ◽  
Novel Approach ◽  
Hydrophobic Peptide

In this research, unzipped sulfanilic acid inspired hydrophobic peptide tube was synthesis by increasing the polarity of sulfanilic acid through nucleophilic attachment of aniline which then provided two reactive sites at the S-terminus. These two sites were then attached with the N-terminal of valine and alanine respectively at an intensity of 1000-1600 of 11 2θ (°). Through π-π stacking at the side chains, the opened ended peptide was linearly arranged to form the unzipped tube. Fourier transform infrared spectroscopy (FTIR) confirm the amine bond formation whiles X-ray diffraction test results confirmed D-spacing 7.36 and 4.44 corresponding 2θ (°)12 and 19.97 respectively whiles the torsion angles (Ø2) conformations was between-150.5°and-169.2° and-2 between-129.0° and-150.6°. The Thermogravimetric analysis result showed an increase in the rigidity of the bond with an increasing intensity. Finally, Differential scanning calorimetry (DSC) test was carried out to confirm the crystallinity of the structure. Keywords: Sulfanilic acid, hydrophobic Peptide, Unzipped tubes, Nanomaterial

scholarly journals A developmentally regulated membrane protein gene in Dictyostelium discoideum is also induced by heat shock and cold shock.

1988 ◽  
Vol 8 (1) ◽  
pp. 153-159 ◽  
Author(s):  
M Maniak ◽  
W Nellen
Keyword(s):  
Heat Shock ◽  
Membrane Protein ◽  
Rna Processing ◽  
Cold Shock ◽  
Protein Gene ◽  
Nuclear Accumulation ◽  
Control Mechanisms ◽  
Developmentally Regulated ◽  
Hydrophobic Peptide ◽  
Membrane Protein Gene

We have analyzed the expression of the Dictyostelium gene P8A7 which had been isolated as a cDNA clone from an early developmentally regulated gene. The single genomic copy generated two mRNAs which were subject to different control mechanisms: while one mRNA (P8A7S) was regulated like the cell-type-nonspecific late genes, the other one (P8A7L) was induced during development, when cells were allowed to attach to a substrate, and when cells were subjected to stress, such as heat shock and cadmium. Interestingly the same induction was also observed with cold shock. RNA processing was inhibited by heat and cold shock, leading to nuclear accumulation of a precursor. The translated region of the cDNA was common to both mRNAs and encoded an unusually hydrophobic peptide with the characteristics of a membrane protein.

scholarly journals Posttranslational modification and intracellular transport of a trypanosome variant surface glycoprotein.

1986 ◽  
Vol 103 (1) ◽  
pp. 255-263 ◽  
Author(s):  
J D Bangs ◽  
N W Andrews ◽  
G W Hart ◽  
P T Englund
Keyword(s):  
Cell Surface ◽  
Phospholipase C ◽  
Intracellular Transport ◽  
Signal Sequence ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein ◽  
Hydrophobic Peptide ◽  
Membrane Bound ◽  
A Site ◽  
Kinetics Of

After synthesis on membrane-bound ribosomes, the variant surface glycoprotein (VSG) of Trypanosoma brucei is modified by: (a) removal of an N-terminal signal sequence, (b) addition of N-linked oligosaccharides, and (c) replacement of a C-terminal hydrophobic peptide with a complex glycolipid that serves as a membrane anchor. Based on pulse-chase experiments with the variant ILTat-1.3, we now report the kinetics of three subsequent processing reactions. These are: (a) conversion of newly synthesized 56/58-kD polypeptides to mature 59-kD VSG, (b) transport to the cell surface, and (c) transport to a site where VSG is susceptible to endogenous membrane-bound phospholipase C. We found that the t 1/2 of all three of these processes is approximately 15 min. The comparable kinetics of these processes is compatible with the hypotheses that transport of VSG from the site of maturation to the cell surface is rapid and that VSG may not reach a phospholipase C-containing membrane until it arrives on the cell surface. Neither tunicamycin nor monensin blocks transport of VSG, but monensin completely inhibits conversion of 58-kD VSG to the mature 59-kD form. In the presence of tunicamycin, VSG is synthesized as a 54-kD polypeptide that is subsequently processed to a form with a slightly higher Mr. This tunicamycin-resistant processing suggests that modifications unrelated to N-linked oligosaccharides occur. Surprisingly, the rate of VSG transport is reduced, but not abolished, by dropping the chase temperature to as low as 10 degrees C.

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