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Your search keyword '"Aguilar, Marie-Isabel"' showing total 14 results
Start Over Author "Aguilar, Marie-Isabel" Journal biochemistry
14 results on '"Aguilar, Marie-Isabel"'

1. Inhibitors of metalloendopeptidase EC 3.4.24.15 and EC 3.4.24.16 stabilized against proteolysis by the incorporation of beta-amino acids

Author

Steer, David, Lew, Rebecca, Perlmutter, Patrick, Smith, A. Ian, and Aguilar, Marie-Isabel

Subjects
Enzyme inhibitors -- Design and construction, Metalloenzymes -- Research, Amino acids -- Structure-activity relationships, Protease inhibitors -- Analysis, Biological sciences, Chemistry
Abstract

Results show that incorporation of beta-amino acids into the design of inhibitors of metalloendopeptidase EP 24.15 and EP 24.16 decreases the inhibitory rate to a low micromolar range. Data show that the inhibitors are resistant to cleavage by peptidase, suggesting the role of beta-amino acids in stabilizing enzyme inhibitors.

Published
2002

2. Electrostatic and hydrophobic forces tether the proximal region of the angiotensin II receptor (AT(sub)1A) carboxyl terminus to anionic lipids

Author

Mozsolits, Henriette, Unabia, Sharon, Ahmad, Ariani, Morton, Craig J., Thomas, Walter G., and Aguilar, Marie-Isabel

Subjects
Angiotensin -- Receptors, Conformational analysis -- Research, Lipid membranes -- Influence, Proteins -- Structure, Biological sciences, Chemistry
Abstract

The proximal carboxyl terminus of the angiotensin II receptor is associated with the cell membrane by tethering through a high-affinity, anioninc phospholipid that enhances the amphipathic helicity of the terminus, indicating that this region of the terminus is sensitive to hydrophobic environment.

Published
2002

3. The toxicity of prion protein fragment PrP(106-126) is not mediated by membrane permeabilization as shown by a M112W substitution

Author

Henriques, Sonia Troeira, Pattenden, Leonard Keith, Aguilar, Marie-Isabel, and Castanho, Miguel A.R.B.

Subjects
Biological transport -- Analysis, Prions -- Chemical properties, Prions -- Structure, Protein binding -- Analysis, Biological sciences, Chemistry
Abstract

The affinity of prion protein, PrP for membranes is increased by modifying it with a M112W substitution which however showed that the membrane permeability is not increased. The toxicity of prion proteins is not a consequence of peptide-membrane interaction.

Published
2009

4. Effect of antimicrobial peptides from Australian tree frogs on anionic phospholipid membranes

Author

Gehman John D., Fiona Luc, Hall, Kristopher, Tzong-Hsien Lee, Boland, Martin P., Pukala, Tara L., Bowie, John H., and Aguilar, Marie-Isabel

Subjects
Acylation -- Analysis, Peptides -- Chemical properties, Phospholipids -- Chemical properties, Phospholipids -- Structure, Biological sciences, Chemistry
Abstract

Deuterated dimyristoylphosphatidylcholine [([d.sub.54]-DMPC] was used to probe the effect of the peptides on the order of the lipid acyl chains and dynamics of the phospholipid head groups. The results demonstrate several important differences when anionic phospholipids are included in model membranes and also provide insight into interaction between antimicrobial peptide and bacterial membranes

Published
2008

5. Binding of amyloidogenic transthyretin to the plasma membrane alters membrane fluidity and induces neurotoxicity

Author

Xu Hou, Richardson, Samantha J., Aguilar, Marie-Isabel, and Small, David H.

Subjects
Amyloid beta-protein -- Research, Membrane proteins -- Research, Biological sciences, Chemistry
Abstract

The mechanism of transthyretin (TTR) amyloid neurotoxicity on SH-SY5Y neuroblastoma cells is examined. The results reveal that the TTR can bind to the plasma membrane and cause a change in membrane fluidity.

Published
2005

6. Strongly altered receptor binding properties in PP and NPY chimeras are accompanied by changes in structure and membrane binding

Author

Lerch, Mirjam, Kamimori, Hiroshi, Folkers, Gerd, Aguilar, Marie-Isabel, Beck-Sickinger, Annette G., and Zerbe, Oliver

Subjects
Binding proteins -- Research, Chimeras (Organisms) -- Structure, Chimeras (Organisms) -- Genetic aspects, Biological sciences, Chemistry
Abstract

Surface plasmon resonance is used to determine whether the chimeric peptides display largely altered membrane association affinities. The results indicate that the differences in receptor binding properties between the chimeras and their parental peptides are most likely due to changes in the conformation of the micelle-bound peptides.

Published
2005

7. Influence of tryptophan on lipid binding of linear amphipathic cationic antimicrobial peptides

Author

Jin, Yi, Mozsolits, Henriette, Hammer, Janet, Zmuda, Erik, Zhu, Fang, Zhang, Yu, Aguilar, Marie Isabel, and Blazyk, Jack

Subjects
Tryptophan -- Influence, Tryptophan -- Physiological aspects, Structure-activity relationships (Biochemistry) -- Analysis, Peptides -- Physiological aspects, Anti-infective agents -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research shows that analogues of the amphipathic beta-sheet structure forming peptides, which contain tryptophan, exhibit strikingly different lipid binding and lytic activity between the alpha-helical and beta-sheet peptides than the parent peptides without tryptophan residues. However, both peptide types show similar antimicrobial activity.

Published
2003

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