Publications by authors named "Nicolas Kosa"
Article Synopsis
- * The researchers introduce a hybrid approach that combines computational modeling with experimental testing to optimize peptides through iterative machine learning.
- * They successfully applied this method to find unique peptide substrates for a specific enzyme, showing that machine learning can improve peptide selection beyond traditional biological screening methods.
Bioo Scientific Corp. has developed a rapid enzymatic quantitative assay for the determination of histamine in seafood. Fresh/frozen tuna, canned tuna, pouched tuna, and frozen mahi mahi samples were used for the validation study under the specific guidelines of the AOAC Research Institute Performance Tested MethodsSM program.
View Article and Find Full Text PDFWe present a spherical micelle generated in a three-step sequence in which a farnesyl-pantetheine conjugate is phosphorylated, adenylated, and phosphorylated once more to generate a farnesyl-CoA amphiphile that self-assembles into spherical micelles. A sphere-to-fibril morphological switch is achieved by enzymatically transferring the farnesyl group of the farnesyl-CoA micelle onto a peptide via phosphopantetheinyl transferase to generate a peptide amphiphile. Each step in the sequence is followed with characterization by HPLC, MS, TEM, and DLS.
View Article and Find Full Text PDFArticle Synopsis
- 4'-Phosphopantetheinyl transferases (PPTases) are enzymes that modify carrier proteins and are crucial for biological processes across all life forms.
- The study focuses on the Sfp-type PPTases from Mycobacterium tuberculosis and Mycobacterium ulcerans, revealing unique structural features that differentiate them from other known PPTases.
- These findings indicate that Mycobacterial PPTases may be promising targets for developing new treatments against infections caused by these pathogens.
The post-translational modifying enzymes phophopantetheinyl transferase and acyl carrier protein hydrolase have shown utility in the functional modification of acyl carrier proteins. Here we develop these tools as immobilized biocatalysts on agarose supports. New utility is imparted through these methods, enabling rapid and label-independent protein purification.
View Article and Find Full Text PDFEvaluation of new acyl carrier protein hydrolase (AcpH, EC 3.1.4.
View Article and Find Full Text PDF4'-Phosphopantetheinyl transferases (PPTases) catalyze a post-translational modification essential to bacterial cell viability and virulence. We present the discovery and medicinal chemistry optimization of 2-pyridinyl-N-(4-aryl)piperazine-1-carbothioamides, which exhibit submicromolar inhibition of bacterial Sfp-PPTase with no activity toward the human orthologue. Moreover, compounds within this class possess antibacterial activity in the absence of a rapid cytotoxic response in human cells.
View Article and Find Full Text PDFArticle Synopsis
- The study shows how a specific chemical modification can be added and removed from proteins, allowing for better visualization and manipulation of these proteins.
- Researchers focus on a process involving a protein from E. coli called acyl carrier protein, using a technique for post-translational modification.
- The method allows them to label different versions of this protein for in-depth analysis using NMR, highlighting how proteins interact with their substrates.