Can an inhibitor retain activity in plasmin-rich settings where degradable substrates are limited?
The university describes a BPTI-derived synthetic peptide engineered for plasmin resistance. Its listing reports stability after 48 hours in the specified incubation assay and reduced ascites in xenograft models relative to BPTI. Oncology and hemostasis uses are proposed applications.
Plasmin participates in fibrinolysis and can affect the tumor microenvironment. BPTI is a proteinase-inhibitor scaffold; the disclosure focuses on a more stable peptide-derived approach.
Evidence and methods
The disclosure reports an incubation stability comparison and preclinical xenograft observations. It does not provide a full peer-reviewed experimental report for the claimed applications.
Plasmin resistance is reported
UC Davis reports resistance to degradation after 48 hours of plasmin incubation in its described assay.
Ascites result is preclinical
The listing reports a xenograft-model comparison against BPTI, not a clinical outcome.
Patent pending
The technology page gives patent-pending status without a published application number.
Inside the study
Stability as a design constraint
The UC disclosure emphasizes resistance to proteolytic breakdown and describes assays in which the synthetic BPTI-derived peptide retains activity in a plasmin-rich environment.
Interpretation
The intended action is durable plasmin inhibition. Fusion to tumor-targeting moieties and surgical hemostasis are proposed use cases, not demonstrated deployments.
Evidence stage
A technology-transfer description with reported preclinical observations. No human therapeutic or surgery benefit is established.
Paper and research team
Contributors
Inventors are listed in the linked technology record.