Kansas State University Research Foundation

Aruni P Malalasekera

Stefan H Bossmann

Deryl L Troyer

Hongwang Wang

Madumali Kalubowilage

Sebastian O Wendel

Thilani N Samarakoon

Gaohong Zhu

Methods for detecting biomarkers of inflammation, infection, and/or bacterial activity in dairy production, which indicate issues with the milk itself or issues related to the health of the cow. The methods generally comprise contacting a milk sample with a nanoplatform assembly to create an assay solution, and detecting spectral changes in the assay solution that are triggered by enzymatic activity (when present) in the sample. The nanoplatform assembly comprises a first particle, a second particle, and a linkage therebetween, wherein the linkage comprises a protease consensus sequence (the sequence of amino acids cleaved by the protease), or an ester linkage (cleaved by a protease or lipase). A plurality of second particles can also be linked to the first particle. Test strips are also described, which undergo a visual color change in the presence of the target enzyme in the milk sample.

Nanosensors for detecting enzymatic activity in dairy production

A nanoplatform assembly for detection of arginase, indoleamine 2,3-dioxygenase 1, and/or tryptophan 2,3-dioxygenase. The nanoplatform comprises an oligopeptide, which is used as a linker between two particles. More preferably, the linker is comprised of an oligopeptide containing a substrate for the target enzyme, where the substrate is chemically or physically modified by the target enzyme (but not cleaved). A central particle with a plurality of oligopeptide-tethered detectable particles and a plurality of directly attached detectable particles is described. Posttranslational modification of the oligopeptide leads to changes in the detectable signals from the first and/or second particles in the nanoplatform, which can be correlated to enzyme activity and concentration.

Nanoplatforms for arginase, indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase detection by posttranslational modification

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Manhattan, KS, United States of America

Aruni P Malalasekera