ArticleProceedings of the National Academy of Sciences of the United States of America2012
Unique motifs and hydrophobic interactions shape the binding of modified DNA ligands to protein targets.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.
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Who cites it
134 citing papers in PubMed.
- Trial
- Defining the serum proteomic signature of hepatic steatosis, inflammation, ballooning and fibrosis in non-alcoholic fatty liver disease.Journal of hepatology · 2023Trial
- Trial
- Aptamer-Based Platforms for Human Aging Biomarkers: Multiplexed Proteomics, Biosensors and Translational Perspectives.International journal of molecular sciences · 2026Review
- Data-Driven Electrochemistry Reveals the Impact of Hydrophobicity on Aptamer Cross-Reactivity.ACS measurement science au · 2026Article
- Click Capture SELEX for the Identification of Click-Modified Aptamers Targeting Small Molecules in Solution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Stability modification of therapeutic aptamers: from biostability bottlenecks to nuclease-resistant construct design.RSC chemical biology · 2026Review
- Combinatorial and rational synthesis of complex, base-modified aptamer libraries on microarrays.RSC advances · 2026Article
- In Silico Study of Anti-CD40 DNA Aptamers as Vaccine Adjuvants for Chickens.International journal of molecular sciences · 2026Article
- Placental Protein Release and Uptake From the Fetal Circulation in Healthy Term Pregnancies-A Human In Vivo Exploratory Study.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- CD25-Targeted Aptamer-Drug Conjugate for the Treatment of CD25-Expressing Hematological Malignancies.Pharmaceutics · 2026Article
- Chemically modified DNA aptamers and DNAzymes for expanded functional capabilities.Chemical science · 2026Review
- PRIMED: predicting DNA binding residues by leveraging pre-trained protein language models.Frontiers in artificial intelligence · 2026Article
- Article
- Evaluation of Nanoparticle-Based Plasma Enrichment on Individuals with Primary and Metastatic Pancreatic Cancer.Cancers · 2025Article
- Versatile Enzymatic Approach for Truncation, Labeling, and Mutation of Nucleobase-Modified Aptamers Demonstrated on Indole-Modified β-Conglutin Aptamer.Chembiochem : a European journal of chemical biology · 2025Article
- Nucleic acid aptamers in orthopedic diseases: promising therapeutic agents for bone disorders.Bone research · 2025Review
- Polymerase Synthesis of Hypermodified DNA Displaying a Combination of Thiol, Hydroxyl, Carboxylate, and Imidazole Functional Groups in the Major Groove.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Review
- Using aptamers for targeted delivery of RNA therapies.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Review
74 more citing papers are in PubMed but not listed here.
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Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selection of aptamers from nucleic acid libraries by in vitro evolution represents a powerful method of identifying high-affinity ligands for a broad range of molecular targets. Nevertheless, a sizeable fraction of proteins remain difficult targets due to inherently limited chemical diversity of nucleic acids. We have exploited synthetic nucleotide modifications that confer protein-like diversity on a nucleic acid scaffold, resulting in a new generation of binding reagents called SOMAmers (Slow Off-rate Modified Aptamers). Here we report a unique crystal structure of a SOMAmer bound to its target, platelet-derived growth factor B (PDGF-BB). The SOMAmer folds into a compact structure and exhibits a hydrophobic binding surface that mimics the interface between PDGF-BB and its receptor, contrasting sharply with mainly polar interactions seen in traditional protein-binding aptamers. The modified nucleotides circumvent the intrinsic diversity constraints of natural nucleic acids, thereby greatly expanding the structural vocabulary of nucleic acid ligands and considerably broadening the range of accessible protein targets.
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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.