8 results match your criteria: "7300 Stevenson Center[Affiliation]"

Here we report the use of a microfluidic system to assess the differential metabolomics of murine embryos cultured with endometrial cells-conditioned media (CM). Groups of 10, 1-cell murine B6C3F1 × B6D2F1 embryos were cultured in the microfluidic device. To produce CM, mouse uterine epithelial cells were cultured in potassium simplex optimized medium (KSOM) for 24 h.

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In various polymerization processes, the formation of a wide variety of chains, not only in length but also in chemical composition, broadly complicates comprehensive polymer characterization. In this communication, we compare different stationary and mobile phases for the analysis of complex polymer mixtures via size-exclusion chromatography-mass spectrometry (SEC-MS). To the best of our knowledge, we report novel chromatographic effects for the separation of linear and cyclic oligomers for polyesters (PE) and polyurethanes (PUR).

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Structuring Microbial Metabolic Responses to Multiplexed Stimuli via Self-Organizing Metabolomics Maps.

Chem Biol

May 2015

Department of Chemistry, Vanderbilt University, 7300 Stevenson Center, Nashville, TN 37235, USA; Vanderbilt Institute for Integrative Biosystems Research and Education, Vanderbilt University, 6301 Stevenson Center, Nashville, TN 37235, USA; Vanderbilt Institute of Chemical Biology, Vanderbilt University, 7300 Stevenson Center, Nashville, TN 37235, USA. Electronic address:

Secondary metabolite biosynthesis in microorganisms responds to discrete chemical and biological stimuli; however, untargeted identification of these responses presents a significant challenge. Herein we apply multiplexed stimuli to Streptomyces coelicolor and collect the resulting response metabolomes via ion mobility-mass spectrometric analysis. Self-organizing map (SOM) analytics adapted for metabolomic data demonstrate efficient characterization of the subsets of primary and secondary metabolites that respond similarly across stimuli.

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The K-26 family of bacterial secondary metabolites are N-modified tripeptides terminated by an unusual phosphonate analog of tyrosine. These natural products, produced via three different actinomycetales, are potent inhibitors of human angiotensin-I converting enzyme (ACE). Herein we investigate the interkingdom pharmacology of the K-26 family by synthesizing these metabolites and assessing their potency as inhibitors of both the N-terminal and C-terminal domains of human ACE.

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Microbial genome mining for accelerated natural products discovery: is a renaissance in the making?

J Ind Microbiol Biotechnol

February 2014

Department of Chemistry, Vanderbilt University, 7300 Stevenson Center, Nashville, TN, 37225, USA,

Microbial genome mining is a rapidly developing approach to discover new and novel secondary metabolites for drug discovery. Many advances have been made in the past decade to facilitate genome mining, and these are reviewed in this Special Issue of the Journal of Industrial Microbiology and Biotechnology. In this Introductory Review, we discuss the concept of genome mining and why it is important for the revitalization of natural product discovery; what microbes show the most promise for focused genome mining; how microbial genomes can be mined; how genome mining can be leveraged with other technologies; how progress on genome mining can be accelerated; and who should fund future progress in this promising field.

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Plasmodium falciparum, in addition to scavenging essential fatty acids from its intra- and intercellular environments, possesses a functional complement of type II fatty acid synthase (FAS) enzymes targeted to the apicoplast organelle. Recent evidence suggests that products of the plasmodial FAS II system may be critical for the parasite's liver-to-blood cycle transition, and it has been speculated that endogenously generated fatty acids may be precursors for essential cofactors, such as lipoate, in the apicoplast. beta-Ketoacyl-acyl carrier protein (ACP) synthase III (pfKASIII or FabH) is one of the key enzymes in the initiating steps of the FAS II pathway, possessing two functions in P.

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Synthesis of nucleotide analogues by a promiscuous phosphoribosyltransferase.

Org Lett

October 2007

Department of Chemistry, Vanderbilt University, 7300 Stevenson Center Lane, Nashville, Tennessee 37235, USA.

An Escherichia coli strain overexpressing a mutant variant of a phosphoribosyl transferase was developed as a catalyst for the efficient preparation of a range of purine nucleotide analogues. This system offers an efficient and rapid method for nucleotide analogue synthesis with 100% beta-selectivity, providing analytically pure product in a single purification step.

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