ropocamptide and Hemolysis

ropocamptide has been researched along with Hemolysis* in 2 studies

Other Studies

2 other study(ies) available for ropocamptide and Hemolysis

Article	Year
Structural and Functional Assessment of mBjAMP1, an Antimicrobial Peptide from Branchiostoma japonicum, Revealed a Novel α-Hairpinin-like Scaffold with Membrane Permeable and DNA Binding Activity. Journal of medicinal chemistry, 2018, 12-27, Volume: 61, Issue:24 Here we describe the three-dimensional structure and antimicrobial mechanism of mBjAMP1, an antimicrobial peptide (AMP) isolated from Branchiostoma japonicum. The structure of mBjAMP1 was determined by 2D solution NMR spectroscopy and revealed a novel α-hairpinin-like scaffold stabilized by an intramolecular disulfide bond. mBjAMP1 showed effective growth inhibition and bactericidal activities against pathogenic bacteria but was not cytotoxic to mammalian cells. Antimicrobial mechanism studies using fluorescence-based experiments demonstrated that mBjAMP1 did not disrupt membrane integrity. Laser-scanning confocal microscopy indicated that mBjAMP1 is able to penetrate the bacterial cell membrane without causing membrane disruption. Moreover, gel retardation assay suggested that mBjAMP1 directly binds to bacterial DNA as an intracellular target. Collectively, mBjAMP1 may inhibit biological functions by binding to DNA or RNA after penetrating the bacterial cell membrane, thereby causing cell death. These results suggest that mBjAMP1 may present a promising template for the development of peptide-based antibiotics. Topics: Animals; Antimicrobial Cationic Peptides; Cell Membrane; Circular Dichroism; Disulfides; DNA, Bacterial; Erythrocytes; Gram-Negative Bacteria; Gram-Positive Bacteria; Hemolysis; Lancelets; Magnetic Resonance Spectroscopy; Mice; Microbial Sensitivity Tests; Microscopy, Confocal; Protein Conformation; RAW 264.7 Cells	2018
Non hemolytic short peptidomimetics as a new class of potent and broad-spectrum antimicrobial agents. Bioorganic & medicinal chemistry letters, 2013, Aug-15, Volume: 23, Issue:16 Since the bacterial resistance to antibiotics is increasing rapidly, numerous studies have contributed to the design and synthesis of potent synthetic mimics of antimicrobial peptides (AMPs). In an attempt to find the pharmacophore of short antimicrobial peptidomimetics through systematic tuning of hydrophobic and hydrophilic patterns, we have identified a set of short histidine-derived antimicrobial peptides (SAMPs) with potent and broad-spectrum activity. A combination of high antimicrobial activity against methicillin-resistant Staphylococcus aureus (MRSA), without hemolytic activity and proteolytic stability makes these molecules promising candidates for novel antimicrobial therapeutics. Topics: Anti-Infective Agents; Hemolysis; Methicillin-Resistant Staphylococcus aureus; Microbial Sensitivity Tests; Peptidomimetics; Protein Stability	2013

Article

Year

Structural and Functional Assessment of mBjAMP1, an Antimicrobial Peptide from Branchiostoma japonicum, Revealed a Novel α-Hairpinin-like Scaffold with Membrane Permeable and DNA Binding Activity.

Journal of medicinal chemistry, 2018, 12-27, Volume: 61, Issue:24

Here we describe the three-dimensional structure and antimicrobial mechanism of mBjAMP1, an antimicrobial peptide (AMP) isolated from Branchiostoma japonicum. The structure of mBjAMP1 was determined by 2D solution NMR spectroscopy and revealed a novel α-hairpinin-like scaffold stabilized by an intramolecular disulfide bond. mBjAMP1 showed effective growth inhibition and bactericidal activities against pathogenic bacteria but was not cytotoxic to mammalian cells. Antimicrobial mechanism studies using fluorescence-based experiments demonstrated that mBjAMP1 did not disrupt membrane integrity. Laser-scanning confocal microscopy indicated that mBjAMP1 is able to penetrate the bacterial cell membrane without causing membrane disruption. Moreover, gel retardation assay suggested that mBjAMP1 directly binds to bacterial DNA as an intracellular target. Collectively, mBjAMP1 may inhibit biological functions by binding to DNA or RNA after penetrating the bacterial cell membrane, thereby causing cell death. These results suggest that mBjAMP1 may present a promising template for the development of peptide-based antibiotics.

Topics: Animals; Antimicrobial Cationic Peptides; Cell Membrane; Circular Dichroism; Disulfides; DNA, Bacterial; Erythrocytes; Gram-Negative Bacteria; Gram-Positive Bacteria; Hemolysis; Lancelets; Magnetic Resonance Spectroscopy; Mice; Microbial Sensitivity Tests; Microscopy, Confocal; Protein Conformation; RAW 264.7 Cells

2018

Non hemolytic short peptidomimetics as a new class of potent and broad-spectrum antimicrobial agents.

Bioorganic & medicinal chemistry letters, 2013, Aug-15, Volume: 23, Issue:16

Since the bacterial resistance to antibiotics is increasing rapidly, numerous studies have contributed to the design and synthesis of potent synthetic mimics of antimicrobial peptides (AMPs). In an attempt to find the pharmacophore of short antimicrobial peptidomimetics through systematic tuning of hydrophobic and hydrophilic patterns, we have identified a set of short histidine-derived antimicrobial peptides (SAMPs) with potent and broad-spectrum activity. A combination of high antimicrobial activity against methicillin-resistant Staphylococcus aureus (MRSA), without hemolytic activity and proteolytic stability makes these molecules promising candidates for novel antimicrobial therapeutics.

Topics: Anti-Infective Agents; Hemolysis; Methicillin-Resistant Staphylococcus aureus; Microbial Sensitivity Tests; Peptidomimetics; Protein Stability

2013