Mahalka et al., 2009 - Google Patents
Binding of amphipathic α-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and LMahalka et al., 2009
View HTML- Document ID
- 10435365682961732623
- Author
- Mahalka A
- Kinnunen P
- Publication year
- Publication venue
- Biochimica et Biophysica Acta (BBA)-Biomembranes
External Links
Snippet
Temporins constitute a family of amphipathic α-helical antimicrobial peptides (AMP) and contain some of the shortest cytotoxic peptides, comprised of only 10–14 residues. General characteristics of temporins parallel those of other AMP, both in terms of structural features …
- 101710004799 sm-amp-x 0 title abstract description 114
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4723—Cationic antimicrobial peptides, e.g. defensins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/775—Apolipopeptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Mahalka et al. | Binding of amphipathic α-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and L | |
Lequin et al. | Dermaseptin S9, an α-helical antimicrobial peptide with a hydrophobic core and cationic termini | |
Gottler et al. | Structure, membrane orientation, mechanism, and function of pexiganan—a highly potent antimicrobial peptide designed from magainin | |
Chan et al. | Tryptophan-and arginine-rich antimicrobial peptides: structures and mechanisms of action | |
Joshi et al. | Interaction studies of novel cell selective antimicrobial peptides with model membranes and E. coli ATCC 11775 | |
Haney et al. | Solution NMR studies of amphibian antimicrobial peptides: linking structure to function? | |
Nicolas et al. | Peptides as weapons against microorganisms in the chemical defense system of vertebrates | |
Mant et al. | De Novo designed amphipathic α-helical antimicrobial peptides incorporating dab and dap residues on the polar face to treat the gram-negative pathogen, Acinetobacter baumannii | |
Nascimento et al. | Antimicrobial peptides from anurans skin secretions | |
Pasupuleti et al. | Rational design of antimicrobial C3a analogues with enhanced effects against Staphylococci using an integrated structure and function-based approach | |
Kondejewski et al. | Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework | |
Pedron et al. | Novel designed VmCT1 analogs with increased antimicrobial activity | |
Nam et al. | 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 | |
McDonald et al. | Structure–function relationships in histidine-rich antimicrobial peptides from Atlantic cod | |
Crusca Jr et al. | Influence of N‐terminus modifications on the biological activity, membrane interaction, and secondary structure of the antimicrobial peptide hylin‐a1 | |
Nan et al. | Antimicrobial activity, bactericidal mechanism and LPS‐neutralizing activity of the cell‐penetrating peptide pVEC and its analogs | |
Shang et al. | Design of potent, non‐toxic antimicrobial agents based upon the structure of the frog skin peptide, Temporin‐1CEb from Chinese brown frog, Rana chensinensis | |
Vanhoye et al. | Membrane association, electrostatic sequestration, and cytotoxicity of Gly-Leu-rich peptide orthologs with differing functions | |
Libardo et al. | Central role of the copper-binding motif in the complex mechanism of action of ixosin: enhancing oxidative damage and promoting synergy with ixosin B | |
Dubovskii et al. | Novel lynx spider toxin shares common molecular architecture with defense peptides from frog skin | |
Dennison et al. | Low pH enhances the action of maximin H5 against Staphylococcus aureus and helps mediate lysylated phosphatidylglycerol-induced resistance | |
Lee et al. | Salt‐resistant homodimeric bactenecin, a cathelicidin‐derived antimicrobial peptide | |
Cardoso et al. | Peptides containing d-amino acids and retro-inverso peptides: general applications and special focus on antimicrobial peptides | |
Mangoni et al. | Biological characterization and modes of action of temporins and bombinins H, multiple forms of short and mildly cationic anti‐microbial peptides from amphibian skin | |
Garcia et al. | Biosynthesis and antimicrobial evaluation of backbone-cyclized α-defensins |