Nutritional and Clinical Glycomics Research
Carlito Lebrilla is elected to the board of US HUPO. See the news here!
http://www.ushupo.org/Portals/0/Board/PRESS%20RELEASE%20April%202013.pdf
Congrats to Renee Ruhaak for being selected for a Agilent Travel award for the upcoming ASMS conference!
http://www.chem.agilent.com/en-US/promotions/Pages/SteveBergerAward.aspx
Dallas, D. C., et al. (2013). “Extensive in vivo human milk peptidomics reveals specific proteolysis yielding protective antimicrobial peptides.” J Proteome Res.
Milk is traditionally considered an ideal source of the basic elemental nutrients required by infants. More detailed examination is revealing that milk represents a more functional ensemble of components with benefits to both infants and mothers. A comprehensive peptidomics method was developed and used to analyze human milk yielding an extensive array of protein products present in the fluid. Over 300 milk peptides were identified originating from major and many minor protein components of milk. As expected, the majority of peptides derived from beta-casein, however no peptide fragments from the major milk proteins lactoferrin, alpha-lactalbumin and secretory immunoglobulin A were identified. Proteolysis in the mammary gland is selective-released peptides were drawn only from specific proteins and typically from only select parts of the parent sequence. A large number of the peptides showed significant sequence overlap with peptides with known antimicrobial or immunomodulatory functions. Antibacterial assays showed the milk peptide mixtures inhibited the growth of Escherichia coli and Staphylococcus aureus. The pre-digestion of milk proteins and the consequent release antibacterial peptides may provide a selective advantage through evolution by protecting both the mother’s mammary gland and her nursing offspring from infection.
Latest Publications from the Lebrilla Team!
Hua, S., et al. (2013). “Isomer-Specific LC/MS and LC/MS/MS Profiling of the Mouse Serum N-Glycome Reveals a Number of Novel Sialylated N-Glycans.” Anal Chem.
Mice are the premier mammalian models for studies of human physiology and disease, bearing extensive biological similarity to humans with far fewer ethical, economic, or logistic complications. To facilitate glycomic studies based on the mouse model, we comprehensively profiled the mouse serum N-glycome using isomer-specific nano-LC/MS and -LC/MS/MS. N-glycans were identified by accurate mass MS and structurally elucidated by MS/MS. Porous graphitized carbon nano-LC was able to separate out nearly 300 N-linked glycan compounds (including isomers) from just over 100 distinct N-linked glycan compositions. Additional MS/MS structural analysis was performed on a number of novel N-glycans, revealing the structural characteristics of modifications such as dehydration, O-acetylation, and lactylation. Experimental findings were combined with known glycobiology to generate a theoretical library of all biologically-possible mouse serum N-glycan compositions. The library may be used for automated identification of complex mixtures of mouse N-glycans, with possible applications to a wide range of mouse-related research endeavors, including pharmaceutical drug development and biomarker discovery.
Ruhaak, L. R., et al. (2013). “Chip-based nLC-TOF-MS is a highly stable technology for large-scale high-throughput analyses.” Anal Bioanal Chem.
Many studies focused on the discovery of novel biomarkers for the diagnosis and treatment of disease states are facilitated by mass spectrometry-based technology. HPLC coupled to mass spectrometry is widely used; miniaturization of this technique using nano-liquid chromatography (LC)-mass spectrometry (MS) usually results in better sensitivity, but is associated with limited repeatability. The recent introduction of chip-based technology has significantly improved the stability of nano-LC-MS, but no substantial studies to verify this have been performed. To evaluate the temporal repeatability of chip-based nano-LC-MS analyses, N-glycans released from a serum sample were repeatedly analyzed using nLC-PGC-chip-TOF-MS on three non-consecutive days. With an average inter-day coefficient of variation of 4 %, determined on log10-transformed integrals, the repeatability of the system is very high. Overall, chip-based nano-LC-MS appears to be a highly stable technology, which is suitable for the profiling of large numbers of clinical samples for biomarker discovery.
Green, M.K. and C.B. Lebrilla, Ion-molecule reactions as probes of gas-phase structures of peptides and proteins. Mass Spectrom Rev, 1997. 16(2): p. 53-71.
Hu, H., S.G. Penn, C.B. Lebrilla, and P.H. Brown, Isolation and characterization of soluble boron complexes in higher plants. The mechanism of phloem mobility of boron.. The mechanism of phloem mobility of boron. Plant Physiol, 1997. 113(2): p. 649-55.
Penn, S.G., H. Hu, P.H. Brown, and C.B. Lebrilla, Direct analysis of sugar alcohol borate complexes in plant extracts by matrix-assisted laser desorption ionization fourier transform mass spectrometry.. Anal Chem, 1997. 69(13): p. 2471-7.
Tseng, K., L.L. Lindsay, S. Penn, J.L. Hedrick, and C.B. Lebrilla, Characterization of neutral oligosaccharide-alditols from Xenopus laevis egg jelly coats by matrix-assisted laser desorption Fourier transform mass spectrometry.. Anal Biochem, 1997. 250(1): p. 18-28.
Wisner, E.R., K.L. Aho-Sharon, M.J. Bennett, S.G. Penn, C.B. Lebrilla, and M.H. Nantz, A modular lymphographic magnetic resonance imaging contrast agent- contrast enhancement with DNA transfection potential.. J Med Chem, 1997. 40(25): p. 3992-6.
Pruesse, T., C.B. Lebrilla, T. Drewello, and H. Schwarz, Iron(I)-induced demethanation of tert-butyl-substituted nitriles in the gas phase. A case of remote functionalization of carbon-carbon bonds.. J Am Chem Soc, 1988. 110(18): p. 5986-93.
Lebrilla, C.B., D.T. Wang, R.L. Hunter, and R.T. McIver, Jr., Detection of mass 31,830 ions with an external ion source Fourier transform mass spectrometer.. Anal Chem, 1990. 62(8): p. 878-80.
Carroll, J.A., L. Ngoka, C.G. Beggs, and C.B. Lebrilla, Liquid secondary ion mass spectrometry Fourier transform mass spectrometry of oligosaccharide anions.. Anal Chem, 1993. 65(11): p. 1582-7.
1. Ngoka, L. C.; Gal, J. F.; Lebrilla, C. B., Effects of cations and charge types on the metastable decay rates of oligosaccharides.. Analytical chemistry 1994, 66 (5), 692-8.
1. Wu, J.; Fannin, S. T.; Franklin, M. A.; Molinski, T. F.; Lebrilla, C. B., Exact mass determination for elemental analysis of ions produced by matrix-assisted laser desorption.. Analytical chemistry 1995, 67 (20), 3788-92.
Carroll, J.A., S.G. Penn, S.T. Fannin, J. Wu, M.T. Cancilla, M.K. Green, and C.B. Lebrilla, A dual vacuum chamber fourier transform mass spectrometer with rapidly interchangeable LSIMS, MALDI, and ESI sources- initial results with LSIMS and MALDI.. Anal Chem, 1996. 68(10): p. 1798-804.
Franklin, M.A., S.G. Penn, C.B. Lebrilla, T.H. Lam, I.N. Pessah, and T.F. Molinski, Bastadin 20 and Bastadin O-Sulfate Esters from Ianthella basta- Novel Modulators of the Ry1R FKBP12 Receptor Complex. J Nat Prod, 1996. 59(12): p. 1121-7.
Penn, S.G., M.T. Cancilla, and C.B. Lebrilla, Collision-induced dissociation of branched oligosaccharide ions with analysis and calculation of relative dissociation thresholds.. Anal Chem, 1996. 68(14): p. 2331-9.
Wu, J., C. Chen, M.J. Kurth, and C.B. Lebrilla, Mass spectrometric analyses of beta-ketolactone oligomers, macrocyclic or catenane structures Anal Chem, 1996. 68(1): p. 38-45.
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