Unknown

Dataset Information

0

How nature morphs peptide scaffolds into antibiotics.


ABSTRACT: The conventional notion that peptides are poor candidates for orally available drugs because of protease-sensitive peptide bonds, intrinsic hydrophilicity, and ionic charges contrasts with the diversity of antibiotic natural products with peptide-based frameworks that are synthesized and utilized by Nature. Several of these antibiotics, including penicillin and vancomycin, are employed to treat bacterial infections in humans and have been best-selling therapeutics for decades. Others might provide new platforms for the design of novel therapeutics to combat emerging antibiotic-resistant bacterial pathogens.

SUBMITTER: Nolan EM 

PROVIDER: S-EPMC2846400 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

How nature morphs peptide scaffolds into antibiotics.

Nolan Elizabeth M EM   Walsh Christopher T CT  

Chembiochem : a European journal of chemical biology 20090101 1


The conventional notion that peptides are poor candidates for orally available drugs because of protease-sensitive peptide bonds, intrinsic hydrophilicity, and ionic charges contrasts with the diversity of antibiotic natural products with peptide-based frameworks that are synthesized and utilized by Nature. Several of these antibiotics, including penicillin and vancomycin, are employed to treat bacterial infections in humans and have been best-selling therapeutics for decades. Others might provi  ...[more]

Similar Datasets

| S-EPMC3795957 | biostudies-literature
| S-EPMC7355828 | biostudies-literature
| S-EPMC7773004 | biostudies-literature
| S-EPMC10977697 | biostudies-literature
| S-EPMC3216106 | biostudies-literature
| S-EPMC6389178 | biostudies-literature
| S-EPMC5407947 | biostudies-literature
| S-EPMC7431008 | biostudies-literature
| S-EPMC2923358 | biostudies-literature
| S-EPMC9855121 | biostudies-literature