Nutritional and Clinical Glycomics Research

Category: Uncategorized (Page 4 of 6)

New paper!

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.

 

1997 Publications

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.

1996 Publications

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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