ArticleBiochimica et biophysica acta2014
Asteropsins B-D, sponge-derived knottins with potential utility as a novel scaffold for oral peptide drugs.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Discovery of Ribosomally Synthesized and Post-translationally Modified Knottins from the Deep-Sea SpongeJournal of natural products · 2026Article
- Discovery, biosynthesis, and bioactivities of peptidic natural products from marine sponges and sponge-associated bacteria.Natural product reports · 2025Review
- Discovery and Folding Dynamics of a Fused Bicyclic Cysteine Knot Undecapeptide from the Marine SpongeThe Journal of organic chemistry · 2024Article
- A phage-displayed disulfide constrained peptide discovery platform yields novel human plasma protein binders.PloS one · 2024Article
- Recifin A, Initial Example of the Tyr-Lock Peptide Structural Family, Is a Selective Allosteric Inhibitor of Tyrosyl-DNA Phosphodiesterase I.Journal of the American Chemical Society · 2020Article
- Beyond Antibodies as Binding Partners: The Role of Antibody Mimetics in Bioanalysis.Annual review of analytical chemistry (Palo Alto, Calif.) · 2017Review
- High Proteolytic Resistance of Spider-Derived Inhibitor Cystine Knots.International journal of peptides · 2015Article
- Solution structure of a sponge-derived cystine knot peptide and its notable stability.Journal of natural products · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundKnown linear knottins are unsuitable as scaffolds for oral peptide drug due to their gastrointestinal instability. Herein, a new subclass of knottin peptides from Porifera is structurally described and characterized regarding their potential for oral peptide drug development.
methodsAsteropsins B-D (ASPB, ASPC, and ASPD) were isolated from the marine sponge Asteropus sp. The tertiary structures of ASPB and ASPC were determined by solution NMR spectroscopy and that of ASPD by homology modeling.
resultsThe isolated asteropsins B-D, together with the previously reported asteropsin A (ASPA), compose a new subclass of knottins that share a highly conserved structural framework and remarkable stability against the enzymes in gastrointestinal tract (chymotrypsin, elastase, pepsin, and trypsin) and human plasma.
conclusionAsteropsins can be considered as promising peptide scaffolds for oral bioavailability. GENERAL SIGNIFICANCE: The structural details of asteropsins provide essential information for the engineering of orally bioavailable peptides.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.