Aptamers are short, single-stranded DNA or RNA sequences that fold into 3D shapes capable of binding specific targets—proteins, small molecules, ions, cells, or even complex mixtures—with high affinity and selectivity. Because they are chemically synthesized, readily modified, and often less immunogenic than protein binders, aptamers have matured into a versatile “molecular toolkit” used across diagnostics, biosensing, therapeutics, imaging, and bioprocessing. This article explains APTAMER APPLICATIONS from fundamentals to advanced use-cases, with an emphasis on how teams translate an aptamer sequence into a functioning assay, sensor, drug carrier, or imaging probe. 1) How Aptamers Are Created (Why Selection Method Shapes Applications) Most aptamers are discovered through SELEX (Systematic Evolution of Ligands by EXponential enrichment): iterative rounds of binding, separation, and amplification that enrich sequences best suited to a chosen target and conditions. Modern SELEX variants—such as cell-SELEX, microfluidic SELEX, and capillary electrophoresis SELEX—aim to shorten selection time, improve specificity, and better match real-world sample environments. The practical result is that application performance often depends as much on selection constraints (buffer, temperature, counter-selection targets, matrix effects) as on the final nucleotide sequence. Key takeaway: If the intended application involves serum, saliva, food extracts, or environmental water, designing SELEX conditions to…
Molecular imaging is a family of techniques that visualizes biological processes in living subjects by using probes that bind to specific molecular targets. In nuclear medicine, PET (positron emission tomography) and SPECT (single-photon emission computed tomography) are workhorse modalities because they can detect tiny (trace) amounts of radiolabeled compounds and quantify target-related signals in vivo. Within PET/SPECT, targeted peptides have become a major probe class: short amino-acid sequences engineered to recognize receptors or other biomarkers (often overexpressed in tumors or diseased tissue), then “tagged” with a radionuclide so the binding event becomes imageable. 1) What Makes Peptide Targeting So Useful in PET and SPECT? Peptides sit in a sweet spot between small molecules and antibodies: High affinity and specificity (when well-designed): peptides can be tuned to fit receptor binding pockets or interaction surfaces, producing strong target-to-background contrast. Fast pharmacokinetics: many peptides clear from blood relatively quickly, which can reduce background signal and enable same-day imaging workflows (depending on isotope half-life and probe design). Chemically modular: it’s typically straightforward to add linkers, chelators, or stabilizing modifications without destroying binding—if the chemistry is placed away from the binding “hot spots.” In practice, peptide probes often target cell-surface receptors…
