Immune & Antimicrobial
Proline-rich Antimicrobial Peptides (PrAMPs)
Nearly every peptide in this class kills by rupturing the bacterial membrane. Proline-rich antimicrobial peptides, from insects and cattle, do something subtler: the bacterium imports them through one of its own transporters, and once inside they wedge into the ribosome's exit tunnel so it cannot build proteins — the cell carries in its own poison. In mice with bloodstream infection by multidrug-resistant Acinetobacter, an engineered version called ARV-1502 saved every treated animal while untreated mice and mice given imipenem all died. That engineering is the catch: the natural members have living-animal results only against antibiotic-susceptible strains, and no proline-rich peptide of any kind has been given to a person in any study on file.
Last updated
Mechanism
Imported by bacterial transporters such as SbmA, then bind the ribosomal exit tunnel and block the transition to translation elongation.
Reported effects
What sources associate with this compound. Reported categories, not outcomes we have graded — each would need its own citation and rung.
- Antibacterial research
- Ribosome inhibition studies
- Antibiotic resistance context
Dosing on file unverified
No established human dose
Carried from a source that labels it unverified, and reproduced with that label attached. A record of what is reported, not a recommendation. No citation on this page establishes it.
Literature on file 6
-
animal in vivo
Translocating Proline-Rich Peptides from the Antimicrobial Peptide Bactenecin 7 (2002, cited 173x) graded on: an animal model — read from the indexed abstract — “mice”
-
review or editorial
Therapeutic potential and resistance of proline-rich antimicrobial peptides. graded on: indexed as "Review" - secondary literature, not a study — “Review”
-
review or editorial
New Aspects of Protein Biosynthesis Inhibition by Proline-Rich Antimicrobial Peptides. graded on: indexed as "Review" - secondary literature, not a study — “Review”
-
review or editorial
Host defense peptides as a new drug lead to a strategy for inflammatory bowel disease. graded on: indexed as "Review" - secondary literature, not a study — “Review”
-
in vitro
Molecular Determinants of Ribosome Binding for the Antimicrobial Peptide Pdi1. graded on: an in-vitro system — read from the indexed abstract — “assay”
-
animal in vivo
The genetic fusion of thaumatin-like proteins with antimicrobial peptides or receptor-like kinases at different evolutionary time points contributes to plant resistance against Sclerotinia disease. graded on: an animal model — read from the indexed abstract — “transgenic”
Notes unverified prose
PL-5 spray Phase 3 (China); B7-005 preclinical; no approved human therapeutic; MIC ≤25 µM in vitro; preclinical
Not on file 9
8 of the 8 fields we track hold nothing on this record, and each says why. 1 further absence is named below. A blank field is a bug; a named absence is a finding.
- molecular weightnothing we hold supplies it
- molecular formulanothing we hold supplies it
- CAS registry numbernothing we hold supplies it
- PubChem identifiernothing we hold supplies it
- amino-acid sequencenothing we hold supplies it
- SMILES stringnothing we hold supplies it
- InChInothing we hold supplies it
- InChI keynothing we hold supplies it
- half-lifenothing we hold supplies it
Each field links to every other record missing the same thing. The full ledger holds 765 gaps across 163 records.