PR1P — Preclinical research guide.
PR1P is a 12-amino-acid peptide derived from Prominin-1 that stabilises and boosts VEGF (vascular endothelial growth factor) signalling. In preclinical mouse models it reduced alveolar cell death in emphysema and, separately, reduced neutrophil-driven lung inflammation in acute lung injury.
- 12-amino-acid peptide derived from a VEGF-binding region of Prominin-1, designed to bind VEGF and boost its receptor signalling.
- Protects VEGF from degradation by inflammatory proteases (elastase, plasmin), preventing formation of pro-inflammatory VEGF fragments.
- In mouse emphysema models, inhaled PR1P reduced alveolar epithelial apoptosis and elastase-driven tissue destruction.
- Separately reduced neutrophil migration and inflammatory cytokines in murine acute lung injury models (LPS, bleomycin and acid-induced).
- Preclinical only — no human trials conducted; not manufactured or sold as a research or clinical compound.
What is PR1P?
PR1P (Prominin-1-Derived Peptide) is a synthetic 12-amino-acid peptide engineered from a VEGF-binding region on the second extracellular domain of Prominin-1, a five-transmembrane glycoprotein with angiogenic properties. It was designed by researchers to bind vascular endothelial growth factor (VEGF) directly and increase its binding to VEGF receptor-2 (VEGFR2) on endothelial and epithelial cells, amplifying a survival signalling pathway that is disrupted in several lung diseases.
How does it work?
Emphysema and related lung diseases are associated with dysregulated VEGF signalling and increased programmed cell death (apoptosis) of the cells lining the alveoli. PR1P binds VEGF within its heparin-binding domain, which does two things: it increases VEGF's binding to VEGFR2 (upregulating the survival signal), and it physically shields VEGF from being cut apart by inflammatory proteases such as elastase and plasmin. That second effect matters because the resulting VEGF fragments are themselves pro-inflammatory — they act as chemical signals that draw neutrophils into the lung, so protecting VEGF from fragmentation also reduces neutrophil-driven inflammation.
What does the research show?
In cultured human bronchial and alveolar epithelial cells, PR1P reduced cigarette-smoke-extract-induced apoptosis. In elastase-induced mouse models of emphysema, inhaled PR1P reduced alveolar destruction and improved measures of lung tissue integrity. In a separate line of experiments, inhaled PR1P reduced neutrophil migration into the airways and lowered inflammatory cytokines (TNF-α, IL-1β, IL-6) across three different murine acute-lung-injury models (LPS, bleomycin, and acid-induced injury). All of this evidence is preclinical — cell culture and animal models — and no human trials of PR1P have been reported.
Is PR1P available for research or purchase?
No. PR1P remains an academic research tool rather than a commercial or clinical compound. It has no assigned CAS number, is not produced by peptide manufacturers, and there is no legitimate supply chain — EU or otherwise — offering it for sale. PeptideCompare documents it here because the underlying VEGF-stabilisation mechanism is a notable direction in lung-disease research, not because it can be sourced.