scholarly journals Isolation and structures of new peptide antibiotics, cirratiomycin A and B.

1982 ◽  
Vol 46 (3) ◽  
pp. 865-867 ◽  
Author(s):  
Teruaki SHIROZA ◽  
Naoyuki EBISAWA ◽  
Kazuo FURIHATA ◽  
Toyoshige ENDO ◽  
Haruo SETO ◽  
...  
Keyword(s):  
Peptide Antibiotics

scholarly journals Amphipathic Peptide Antibiotics with Potent Activity against Multidrug-Resistant Pathogens

Pharmaceutics ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 438
Author(s):  
Jingru Shi ◽  
Chen Chen ◽  
Dejuan Wang ◽  
Ziwen Tong ◽  
Zhiqiang Wang ◽  
...  
Keyword(s):  
Membrane Damage ◽  
Multidrug Resistant ◽  
Peptide Antibiotics ◽  
Biofilm Inhibition ◽  
Amphipathic Peptide ◽  
Host Defense Peptides ◽  
Gram Negative ◽  
Wide Range ◽  
New Antibiotics ◽  
Low Toxicity

The emergence and prevalence of multidrug-resistant (MDR) bacteria have posed a serious threat to public health. Of particular concern are methicillin-resistant Staphylococcus aureus (MRSA) and blaNDM, mcr-1 and tet(X)-positive Gram-negative pathogens. The fact that few new antibiotics have been approved in recent years exacerbates this global crisis, thus, new alternatives are urgently needed. Antimicrobial peptides (AMPs) originated from host defense peptides with a wide range of sources and multiple functions, are less prone to achieve resistance. All these characteristics laid the foundation for AMPs to become potential antibiotic candidates. In this study, we revealed that peptide WW307 displayed potent antibacterial and bactericidal activity against MDR bacteria, including MRSA and Gram-negative bacteria carrying blaNDM-5, mcr-1 or tet(X4). In addition, WW307 exhibited great biofilm inhibition and eradication activity. Safety and stability experiments showed that WW307 had a strong resistance against various physiological conditions and displayed relatively low toxicity. Mechanistic experiments showed that WW307 resulted in membrane damage by selectively targeting bacterial membrane-specific components, including lipopolysaccharide (LPS), phosphatidylglycerol (PG), and cardiolipin (CL). Moreover, WW307 dissipated membrane potential and triggered the production of reactive oxygen species (ROS). Collectively, these results demonstrated that WW307 represents a promising candidate for combating MDR pathogens.

Synthetic Studies on Thiostrepton Family of Peptide Antibiotics: Synthesis of the Tetrasubstituted Dihydroquinoline Portion of Siomycin D1

Heterocycles ◽  
2002 ◽  
Vol 57 (1) ◽  
pp. 111 ◽  
Author(s):  
Kimiko Hashimoto ◽  
Syuhei Higashibayashi ◽  
Tomonori Mori ◽  
Kazuyuki Shinko ◽  
Masaya Nakata
Keyword(s):  
Peptide Antibiotics ◽  
Synthetic Studies

scholarly journals Comparative Analysis of Chromosome-Encoded Microcins

2006 ◽  
Vol 50 (4) ◽  
pp. 1411-1418 ◽  
Author(s):  
María Eloisa Poey ◽  
María F. Azpiroz ◽  
Magela Laviña
Keyword(s):  
Functional Relationship ◽  
General Scheme ◽  
Type I ◽  
Peptide Antibiotics ◽  
Common Features ◽  
Peptide Precursors ◽  
Immunity Genes ◽  
Genetic Clusters ◽  
Secretion Pathways ◽  
Fourth Member

ABSTRACT Microcins are ribosomally synthesized peptide antibiotics that are produced by enterobacterial strains. Although the first studies concentrated on plasmid-encoded activities, in the last years three chromosome-encoded microcins have been described: H47, E492, and M. Here, a new microcin, I47, is presented as a fourth member of this group. Common features exhibited by chromosome-encoded microcins were searched for. The comparison of the genetic clusters responsible for microcin production revealed a preserved general scheme. The clusters essentially comprise a pair of activity-immunity genes which determine antibiotic specificity and a set of microcin maturation and secretion genes which are invariably present and whose protein products are highly homologous among the different producing strains. A strict functional relationship between the maturation and secretion pathways of microcins H47, I47, and E492 was demonstrated through genetic analyses, which included heterologous complementation assays. The peptide precursors of these microcins share a maturation process which implies the addition of a catecholate siderophore of the salmochelin type. Microcins thus acquire the ability to enter gram-negative cells through the catechol receptors. In addition, they employ a common mode of secretion to reach the external milieu by means of a type I export apparatus. The results presented herein lead us to propose that chromosome-encoded microcins constitute a defined subgroup of peptide antibiotics which are strictly related by their modes of synthesis, secretion, and uptake.

Hydrophobic Ion Pairing of Peptide Antibiotics for Processing into Controlled Release Nanocarrier Formulations

2017 ◽  
Vol 15 (1) ◽  
pp. 216-225 ◽  
Author(s):  
Hoang D. Lu ◽  
Paradorn Rummaneethorn ◽  
Kurt D. Ristroph ◽  
Robert K. Prud’homme
Keyword(s):  
Controlled Release ◽  
Ion Pairing ◽  
Peptide Antibiotics ◽  
Hydrophobic Ion Pairing

Advances on chemically modified antimicrobial peptides for generating peptide antibiotics

2021 ◽  
Author(s):  
Samilla Rezende ◽  
karen k.n. oshiro ◽  
Nelson Junior ◽  
Octavio L. Franco ◽  
Marlon Henrique Cardoso
Keyword(s):  
Clinical Trials ◽  
Antimicrobial Peptides ◽  
Bacterial Infections ◽  
Peptide Antibiotics ◽  
Antibiotic Resistant ◽  
Chemically Modified

Antimicrobial peptides (AMPs) are pinpointed as promising molecules against antibiotic-resistant bacterial infections. Nevertheless, there is a discrepancy between the AMP sequences generated and the tangible outcomes in clinical trials. AMPs’...

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