melitten and phenyldehydroalanine

melitten has been researched along with phenyldehydroalanine* in 1 studies

Other Studies

1 other study(ies) available for melitten and phenyldehydroalanine

Article	Year
Alpha,beta-dehydrophenylalanine containing cecropin-melittin hybrid peptides: conformation and activity. Journal of peptide science : an official publication of the European Peptide Society, 2007, Volume: 13, Issue:4 Synthesis and conformational studies of a cecropin-melittin hybrid pentadecapeptide CA(1-7)MEL(2-9), and its three alpha, beta-dehydrophenylalanine (DeltaPhe) containing analogs in water-TFE mixtures are described. DeltaPhe is placed at strategic positions in order to preserve the amphipathicity of the molecule. The wild type CAMEL0 and its three analogs, containing one, two and three DeltaPhe residues namely CAMELDeltaPhe1, CAMELDeltaPhe2 and CAMELDeltaPhe3 respectively were synthesized in solid phase and their conformation determined by CD and NMR. CAMELDeltaPhe2 and CAMELDeltaPhe3 peptides exhibit the presence of 3(10)-helix and beta-turns in the former and only turns in the latter. CAMELDeltaPhe1 peptide was found to have a largely extended conformation. Antibacterial and hemolytic activities of the peptides were also evaluated. CAMELDeltaPhe2 peptide is maximally potent against both Staphylococcus aureus ATCC 259230 and Escherichia coli ATCC 11303. CAMELDeltaPhe1 with a single DeltaPhe at the center shows minimal hemolysis. Topics: Amino Acid Sequence; Animals; Antimicrobial Cationic Peptides; Circular Dichroism; Drug Evaluation, Preclinical; Hemolytic Agents; Magnetic Resonance Spectroscopy; Melitten; Mice; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Phenylalanine; Protein Conformation; Structure-Activity Relationship	2007

Article

Year

Alpha,beta-dehydrophenylalanine containing cecropin-melittin hybrid peptides: conformation and activity.

Journal of peptide science : an official publication of the European Peptide Society, 2007, Volume: 13, Issue:4

Synthesis and conformational studies of a cecropin-melittin hybrid pentadecapeptide CA(1-7)MEL(2-9), and its three alpha, beta-dehydrophenylalanine (DeltaPhe) containing analogs in water-TFE mixtures are described. DeltaPhe is placed at strategic positions in order to preserve the amphipathicity of the molecule. The wild type CAMEL0 and its three analogs, containing one, two and three DeltaPhe residues namely CAMELDeltaPhe1, CAMELDeltaPhe2 and CAMELDeltaPhe3 respectively were synthesized in solid phase and their conformation determined by CD and NMR. CAMELDeltaPhe2 and CAMELDeltaPhe3 peptides exhibit the presence of 3(10)-helix and beta-turns in the former and only turns in the latter. CAMELDeltaPhe1 peptide was found to have a largely extended conformation. Antibacterial and hemolytic activities of the peptides were also evaluated. CAMELDeltaPhe2 peptide is maximally potent against both Staphylococcus aureus ATCC 259230 and Escherichia coli ATCC 11303. CAMELDeltaPhe1 with a single DeltaPhe at the center shows minimal hemolysis.

Topics: Amino Acid Sequence; Animals; Antimicrobial Cationic Peptides; Circular Dichroism; Drug Evaluation, Preclinical; Hemolytic Agents; Magnetic Resonance Spectroscopy; Melitten; Mice; Microbial Sensitivity Tests; Models, Molecular; Molecular Sequence Data; Phenylalanine; Protein Conformation; Structure-Activity Relationship

2007