@article {1442,
	title = {Imaging bacterial peptidoglycan with near-infrared fluorogenic azide probes.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {111},
	year = {2014},
	month = {2014 Apr 15},
	pages = {5456-61},
	abstract = {<p>Fluorescent probes designed for activation by bioorthogonal chemistry have enabled the visualization of biomolecules in living systems. Such activatable probes with near-infrared (NIR) emission would be ideal for in vivo imaging but have proven difficult to engineer. We present the development of NIR fluorogenic azide probes based on the Si-rhodamine scaffold that undergo a fluorescence enhancement of up to 48-fold upon reaction with terminal or strained alkynes. We used the probes for mammalian cell surface imaging and, in conjunction with a new class of cyclooctyne D-amino acids, for visualization of bacterial peptidoglycan without the need to wash away unreacted probe.</p>},
	keywords = {Azides, Fluorescent Dyes, Molecular Imaging, Molecular Probe Techniques, Molecular Structure, Peptidoglycan},
	issn = {1091-6490},
	doi = {10.1073/pnas.1322727111},
	author = {Shieh, Peyton and Siegrist, M Sloan and Cullen, Andrew J and Bertozzi, Carolyn R}
}
@article {1445,
	title = {(D)-Amino acid chemical reporters reveal peptidoglycan dynamics of an intracellular pathogen.},
	journal = {ACS Chem Biol},
	volume = {8},
	year = {2013},
	month = {2013 Mar 15},
	pages = {500-5},
	abstract = {<p>Peptidoglycan (PG) is an essential component of the bacterial cell wall. Although experiments with organisms in vitro have yielded a wealth of information on PG synthesis and maturation, it is unclear how these studies translate to bacteria replicating within host cells. We report a chemical approach for probing PG in vivo via metabolic labeling and bioorthogonal chemistry. A wide variety of bacterial species incorporated azide and alkyne-functionalized d-alanine into their cell walls, which we visualized by covalent reaction with click chemistry probes. The d-alanine analogues were specifically incorporated into nascent PG of the intracellular pathogen Listeria monocytogenes both in vitro and during macrophage infection. Metabolic incorporation of d-alanine derivatives and click chemistry detection constitute a facile, modular platform that facilitates unprecedented spatial and temporal resolution of PG dynamics in vivo.</p>},
	keywords = {Alanine, Click Chemistry, Listeria monocytogenes, Molecular Conformation, Molecular Dynamics Simulation, Peptidoglycan},
	issn = {1554-8937},
	doi = {10.1021/cb3004995},
	author = {Siegrist, M Sloan and Whiteside, Sarah and Jewett, John C and Aditham, Arjun and Cava, Felipe and Bertozzi, Carolyn R}
}
@article {734,
	title = {"Doubly selective" antimicrobial polymers: how do they differentiate between bacteria?},
	journal = {Chemistry},
	volume = {15},
	year = {2009},
	month = {2009 Nov 2},
	pages = {11710-4},
	abstract = {We have investigated how doubly selective synthetic mimics of antimicrobial peptides (SMAMPs), which can differentiate not only between bacteria and mammalian cells, but also between Gram-negative and Gram-positive bacteria, make the latter distinction. By dye-leakage experiments on model vesicles and complementary experiments on bacteria, we were able to relate the Gram selectivity to structural differences of these bacteria types. We showed that the double membrane of E. coli rather than the difference in lipid composition between E. coli and S. aureus was responsible for Gram selectivity. The molecular-weight-dependent antimicrobial activity of the SMAMPs was shown to be a sieving effect: while the 3000 g mol(-1) SMAMP was able to penetrate the peptidoglycan layer of the Gram-positive S. aureus bacteria, the 50000 g mol(-1) SMAMP got stuck and consequently did not have antimicrobial activity.},
	keywords = {Anti-Infective Agents, Biomimetic Materials, Escherichia coli, Microbial Sensitivity Tests, Peptidoglycan, Polymers, Staphylococcus aureus},
	issn = {1521-3765},
	doi = {10.1002/chem.200802558},
	author = {Lienkamp, Karen and Kumar, Kushi-Nidhi and Som, Abhigyan and N{\"u}sslein, Klaus and Tew, Gregory N}
}
