Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus

1993 ◽  
Vol 115 (17) ◽  
pp. 7557-7568 ◽  
Author(s):  
Ursula Mocek ◽  
Andrew R. Knaggs ◽  
Reiko Tsuchiya ◽  
Tom Nguyen ◽  
John M. Beale ◽  
...  
Keyword(s):  
Peptide Antibiotic ◽  
Streptomyces Actuosus

Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus

1988 ◽  
Vol 110 (17) ◽  
pp. 5800-5806 ◽  
Author(s):  
David R. Houck ◽  
Li Chun. Chen ◽  
Paul J. Keller ◽  
John M. Beale ◽  
Heinz G. Floss
Keyword(s):  
Peptide Antibiotic ◽  
Streptomyces Actuosus

ChemInform Abstract: Biosynthesis of the Modified Peptide Antibiotic Nosiheptide in Streptomyces actuosus.

ChemInform ◽  
2010 ◽  
Vol 24 (51) ◽  
pp. no-no
Author(s):  
U. MOCEK ◽  
A. R. KNAGGS ◽  
R. TSUCHIYA ◽  
T. NGUYEN ◽  
J. M. BEALE ◽  
...  
Keyword(s):  
Peptide Antibiotic ◽  
Streptomyces Actuosus

Biosynthesis of the modified peptide antibiotic nosiheptide in Streptomyces actuosus

1987 ◽  
Vol 109 (4) ◽  
pp. 1250-1252 ◽  
Author(s):  
David R. Houck ◽  
Li Chun Chen ◽  
Paul J. Keller ◽  
John M. Beale ◽  
Heinz G. Floss
Keyword(s):  
Peptide Antibiotic ◽  
Streptomyces Actuosus

scholarly journals The Potential of Human Peptide LL-37 as an Antimicrobial and Anti-Biofilm Agent

Antibiotics ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 650
Author(s):  
Kylen E. Ridyard ◽  
Joerg Overhage
Keyword(s):  
Bacterial Infections ◽  
Antimicrobial Properties ◽  
Cross Resistance ◽  
Resistant Bacteria ◽  
Peptide Antibiotic ◽  
Adaptive Responses ◽  
Antibiotic Resistant ◽  
Structural Modifications ◽  
Immobilization Techniques ◽  
Conventional Antibiotics

The rise in antimicrobial resistant bacteria threatens the current methods utilized to treat bacterial infections. The development of novel therapeutic agents is crucial in avoiding a post-antibiotic era and the associated deaths from antibiotic resistant pathogens. The human antimicrobial peptide LL-37 has been considered as a potential alternative to conventional antibiotics as it displays broad spectrum antibacterial and anti-biofilm activities as well as immunomodulatory functions. While LL-37 has shown promising results, it has yet to receive regulatory approval as a peptide antibiotic. Despite the strong antimicrobial properties, LL-37 has several limitations including high cost, lower activity in physiological environments, susceptibility to proteolytic degradation, and high toxicity to human cells. This review will discuss the challenges associated with making LL-37 into a viable antibiotic treatment option, with a focus on antimicrobial resistance and cross-resistance as well as adaptive responses to sub-inhibitory concentrations of the peptide. The possible methods to overcome these challenges, including immobilization techniques, LL-37 delivery systems, the development of LL-37 derivatives, and synergistic combinations will also be considered. Herein, we describe how combination therapy and structural modifications to the sequence, helicity, hydrophobicity, charge, and configuration of LL-37 could optimize the antimicrobial and anti-biofilm activities of LL-37 for future clinical use.

scholarly journals Antimicrobial Peptide Modifications against Clinically Isolated Antibiotic-Resistant Salmonella

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4654
Author(s):  
Suthee Mangmee ◽  
Onrapak Reamtong ◽  
Thareerat Kalambaheti ◽  
Sittiruk Roytrakul ◽  
Piengchan Sonthayanon
Keyword(s):  
Antibacterial Activity ◽  
Hemolytic Activity ◽  
Multidrug Resistant ◽  
Terminal Group ◽  
Scorpion Venom ◽  
Antibiofilm Activity ◽  
Peptide Antibiotic ◽  
Dependent Manner ◽  
C Terminus ◽  
Relationship Of

Antimicrobial peptides are promising molecules to address the global antibiotic resistance problem, however, optimization to achieve favorable potency and safety is required. Here, a peptide-template modification approach was employed to design physicochemical variants based on net charge, hydrophobicity, enantiomer, and terminal group. All variants of the scorpion venom peptide BmKn-2 with amphipathic α-helical cationic structure exhibited an increased antibacterial potency when evaluated against multidrug-resistant Salmonella isolates at a MIC range of 4–8 µM. They revealed antibiofilm activity in a dose-dependent manner. Sheep red blood cells were used to evaluate hemolytic and cell selectivity properties. Peptide Kn2-5R-NH2, dKn2-5R-NH2, and 2F-Kn2-5R-NH2 (variants with +6 charges carrying amidated C-terminus) showed stronger antibacterial activity than Kn2-5R (a variant with +5 charges bearing free-carboxyl group at C-terminus). Peptide dKn2-5R-NH2 (d-enantiomer) exhibited slightly weaker antibacterial activity with much less hemolytic activity (higher hemolytic concentration 50) than Kn2-5R-NH2 (l-enantiomer). Furthermore, peptide Kn2-5R with the least hydrophobicity had the lowest hemolytic activity and showed the highest specificity to Salmonella (the highest selectivity index). This study also explained the relationship of peptide physicochemical properties and bioactivities that would fulfill and accelerate progress in peptide antibiotic research and development.

Tylopeptin B peptide antibiotic in lipid membranes at low concentrations: Self-assembling, mutual repulsion and localization

2021 ◽  
pp. 183585
Author(s):  
Victoria N. Syryamina ◽  
Natalia E. Sannikova ◽  
Marta De Zotti ◽  
Marina Gobbo ◽  
Fernando Formaggio ◽  
...  
Keyword(s):  
Lipid Membranes ◽  
Peptide Antibiotic ◽  
Self Assembling ◽  
Low Concentrations

scholarly journals EM49, A NEW PEPTIDE ANTIBIOTIC

1973 ◽  
Vol 26 (8) ◽  
pp. 444-448 ◽  
Author(s):  
EDWARD MEYERS ◽  
WILLIAM E. BROWN ◽  
PACIFICO A. PRINCIPE ◽  
MARLENE L. RATHNUM ◽  
WILLIAM L. PARKER
Keyword(s):  
Peptide Antibiotic
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