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Isothermal PCR can be performed by imposing a static temperature gradient that continuously circulates reagents through denaturing, annealing, and extension conditions inside a PCR tube. But despite early promise, these systems have yet to demonstrate performance and repeatability sufficient for adoption in validated laboratory tests because the rate‐limiting extension step is inherently short and cannot be increased independently of the other stages in a temperature cycle. Here, a discovery that enables isothermal PCR to be achieved with statistically robust repeatability that meets or exceeds diagnostic assay requirements (false positive/negative rate <8% at 95% confidence) by manipulating the interplay between the DNA replication biochemistry (via the amplicon GC content) and the microscale circulatory flow inside a PCR tube is reported. Surprisingly, optimal performance depends on selecting primer sequences that replicate high GC content amplicons, contradicting established PCR primer design rules. This innovative thermocycling approach accelerates PCR to speeds rivaling ultra‐fast instruments, enabling rapid, repeatable isothermal DNA analysis across a range of targets relevant to diagnostics and pathogen detection. [ABSTRACT FROM AUTHOR]

Discovery of unique peptides that specifically bind to target materials of interest is commonly achieved through biopanning‐based screening of cell libraries having high diversity. However, conventional methods have limitations in the generation of controllable shear stress applied in order to effectively remove weak and unbound cells from a target material. Here, a centrifugal force‐based microfluidic biopanning platform is presented. Using this microfluidic platform, a wide range of shear stress conditions can be generated by simply adjusting the rotation speed of the platform, which provides a precisely controllable wash step. The enhanced circularly permuted outer membrane protein X (eCPX) 3.0 bacterial peptide display library (≈1011 number of cells) is screened, and many isolates that show strong affinity towards gold only, ITO only, or both are successfully obtained through a multiround iterative sorting process. Amino acid contents of the resulting isolates are analyzed to provide a better understanding of the distinctive attributes of these peptides and their specific material‐binding capabilities. This platform is simple and easy to use and can be readily applied to screen microbial libraries against virtually any material surface of interest, which can greatly accelerate the discovery of peptide‐driven biomaterials and the development of hybrid organic–inorganic materials. [ABSTRACT FROM AUTHOR]