ArticleMolecular bioSystems2010
Peptide ligands that use a novel binding site to target both TGF-β receptors.
Article in Molecular bioSystems, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Review
- Versatile Synthesis of Multivalent Porphyrin-Peptide Conjugates by Direct Porphyrin Construction on Resin.Angewandte Chemie (International ed. in English) · 2022Article
- Bifunctional Peptide that Anneals to Damaged Collagen and Clusters TGF-β Receptors Enhances Wound Healing.ACS chemical biology · 2022Article
- Review
- Fluorescent "Turn off-on" Small-Molecule-Monitoring Nanoplatform Based on Dendrimer-like Peptides as Competitors.ACS applied materials & interfaces · 2019Article
- Bacteriophage-based biomaterials for tissue regeneration.Advanced drug delivery reviews · 2019Review
- In Vivo Translation of Peptide-Targeted Drug Delivery Systems Discovered by Phage Display.Bioconjugate chemistry · 2018Review
- In vitro selection technologies to enhance biomaterial functionality.Experimental biology and medicine (Maywood, N.J.) · 2016Review
- Production, Isolation, and Structural Analysis of Ligands and Receptors of the TGF-β Superfamily.Methods in molecular biology (Clifton, N.J.) · 2016Article
- The non-detergent sulfobetaine-201 acts as a pharmacological chaperone to promote folding and crystallization of the type II TGF-β receptor extracellular domain.Protein expression and purification · 2015Article
- Natural velvet antler polypeptide conformation prediction and molecular docking study with TGF-β1 complex.Journal of molecular modeling · 2013Article
- Aptamers and their potential to selectively target aspects of EGF, Wnt/β-catenin and TGFβ-smad family signaling.International journal of molecular sciences · 2013Review
- Small-molecule-modified surfaces engage cells through the αvβ3 integrin.ACS chemical biology · 2012Article
- Spatial control of cell fate using synthetic surfaces to potentiate TGF-beta signaling.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Diversity of phage-displayed libraries of peptides during panning and amplification.Molecules (Basel, Switzerland) · 2011Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The transforming growth factor beta (TGF-β) signaling pathway plays myriad roles in development and disease. TGF-β isoforms initiate signaling by organizing their cell surface receptors TβRI and TβRII. Exploration and exploitation of the versatility of TGF-β signaling requires an enhanced understanding of structure-function relationships in this pathway. To this end, small molecule, peptide, and antibody effectors that bind key signaling components would serve as valuable probes. We focused on the extracellular domain of TβR1 (TβRI-ED) as a target for effector screening. The observation that TβRI-ED can bind to a TGF-β coreceptor (endoglin) suggests that the TβRI-ED may have multiple interaction sites. Using phage display, we identified two peptides LTGKNFPMFHRN (Pep1) and MHRMPSFLPTTL (Pep2) that bind the TβRI-ED (K(d)≈ 10(-5) M). Although our screen focused on TβRI-ED, the hit peptides interact with the TβRII-ED with similar affinities. The peptide ligands occupy the same binding sites on TβRI and TβRII, as demonstrated by their ability to compete with each other for receptor binding. Moreover, neither interferes with TGF-β binding. These results indicate that both TβRI and TβRII possess hot spots for protein-protein interactions that are distinct from those used by their known ligand TGF-β. To convert these compounds into high affinity probes, we exploited the observation that TβRI and TβRII exist as dimers on the cell surface; therefore, we assembled a multivalent ligand. Specifically, we displayed one of our receptor-binding peptides on a dendrimer scaffold. We anticipate that the potent multivalent ligand that resulted can be used to probe the role of receptor assembly in TGF-β function.
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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.