beta-naphthylalanine and Hemolysis

beta-naphthylalanine has been researched along with Hemolysis* in 2 studies

Other Studies

2 other study(ies) available for beta-naphthylalanine and Hemolysis

Article	Year
Boosting salt resistance of short antimicrobial peptides. Antimicrobial agents and chemotherapy, 2013, Volume: 57, Issue:8 The efficacies of many antimicrobial peptides are greatly reduced under high salt concentrations, therefore limiting their use as pharmaceutical agents. Here, we describe a strategy to boost salt resistance and serum stability of short antimicrobial peptides by adding the nonnatural bulky amino acid β-naphthylalanine to their termini. The activities of the short salt-sensitive tryptophan-rich peptide S1 were diminished at high salt concentrations, whereas the activities of its β-naphthylalanine end-tagged variants were less affected. Topics: Amino Acid Sequence; Ampicillin; Anti-Infective Agents; beta-Alanine; Drug Stability; Erythrocytes; Escherichia coli; Hemolysis; Humans; Microbial Sensitivity Tests; Peptides; Serum; Sodium Chloride; Tryptophan	2013
Solution structure of a novel D-naphthylalanine substituted peptide with potential antibacterial and antifungal activities. Biopolymers, 2007, Volume: 88, Issue:5 A new type of Trp-rich peptide, Ac-KWRRWVRWI-NH2, designated as Pac-525, was found to possess improved activity against both gram-positive and negative bacteria. We have synthesized two Pac-525 analogues, D-Pac-525 containing all D-amino acids and D-Nal-Pac-525, the D-Pac-525 analogue with tryptophan replaced by D-beta-naphthylalanine. We have determined the solution structure of D-Nal-Pac-525 bound to membrane-mimetic DPC micelles by two-dimensional NMR methods. The DPC micelle-bound structure of D-Nal-Pac-525 adopts a left-hand alpha-helical segment and the positively charged residues are clustered together to form a hydrophilic patch. The surface electrostatic potential map indicates the three D-beta-naphthylalanines are packed against the peptide backbone and form an amphipathic structure. A variety of biophysical and biochemical experiments, including circular dichroism, fluorescence spectroscopy, and microcalorimetry, were used to show that D-Nal-Pac-525 interacted strongly with negatively charged phospholipid vesicles and induced efficient dye release from these vesicles, suggesting that the strong antimicrobial activity of D-Nal-Pac-525 may be due to interactions with bacterial and fungus membranes. Topics: Anti-Bacterial Agents; Antifungal Agents; beta-Alanine; Calorimetry; Candida albicans; Circular Dichroism; Fluoresceins; Gram-Negative Bacteria; Gram-Positive Bacteria; Hemolysis; Humans; Nuclear Magnetic Resonance, Biomolecular; Peptides; Protein Denaturation; Spectrometry, Fluorescence; Temperature; Titrimetry; Tryptophan	2007

Article

Year

Boosting salt resistance of short antimicrobial peptides.

Antimicrobial agents and chemotherapy, 2013, Volume: 57, Issue:8

The efficacies of many antimicrobial peptides are greatly reduced under high salt concentrations, therefore limiting their use as pharmaceutical agents. Here, we describe a strategy to boost salt resistance and serum stability of short antimicrobial peptides by adding the nonnatural bulky amino acid β-naphthylalanine to their termini. The activities of the short salt-sensitive tryptophan-rich peptide S1 were diminished at high salt concentrations, whereas the activities of its β-naphthylalanine end-tagged variants were less affected.

Topics: Amino Acid Sequence; Ampicillin; Anti-Infective Agents; beta-Alanine; Drug Stability; Erythrocytes; Escherichia coli; Hemolysis; Humans; Microbial Sensitivity Tests; Peptides; Serum; Sodium Chloride; Tryptophan

2013

Solution structure of a novel D-naphthylalanine substituted peptide with potential antibacterial and antifungal activities.

Biopolymers, 2007, Volume: 88, Issue:5

A new type of Trp-rich peptide, Ac-KWRRWVRWI-NH2, designated as Pac-525, was found to possess improved activity against both gram-positive and negative bacteria. We have synthesized two Pac-525 analogues, D-Pac-525 containing all D-amino acids and D-Nal-Pac-525, the D-Pac-525 analogue with tryptophan replaced by D-beta-naphthylalanine. We have determined the solution structure of D-Nal-Pac-525 bound to membrane-mimetic DPC micelles by two-dimensional NMR methods. The DPC micelle-bound structure of D-Nal-Pac-525 adopts a left-hand alpha-helical segment and the positively charged residues are clustered together to form a hydrophilic patch. The surface electrostatic potential map indicates the three D-beta-naphthylalanines are packed against the peptide backbone and form an amphipathic structure. A variety of biophysical and biochemical experiments, including circular dichroism, fluorescence spectroscopy, and microcalorimetry, were used to show that D-Nal-Pac-525 interacted strongly with negatively charged phospholipid vesicles and induced efficient dye release from these vesicles, suggesting that the strong antimicrobial activity of D-Nal-Pac-525 may be due to interactions with bacterial and fungus membranes.

Topics: Anti-Bacterial Agents; Antifungal Agents; beta-Alanine; Calorimetry; Candida albicans; Circular Dichroism; Fluoresceins; Gram-Negative Bacteria; Gram-Positive Bacteria; Hemolysis; Humans; Nuclear Magnetic Resonance, Biomolecular; Peptides; Protein Denaturation; Spectrometry, Fluorescence; Temperature; Titrimetry; Tryptophan

2007