Clues to a Pd/C catalyst’s efficiency can be found on its surface: Identification of an efficient catalyst for the global hydrogenolysis of ether protecting groups

Crawford, Cynda; Qiao, Yan; Liu, Yequn; Huang, Dongmei; Yan, Wenjun; Oscarson, Stefan; Chen, Shuai

doi:10.26434/chemrxiv.12793634.v1

Cited by 1 publication

(1 citation statement)

References 14 publications

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“…The N-phthalimido protecting group was then selectively removed in the presence of the 6-O-acetylation pattern using ethylenediamine, followed by formation of the N-Boc protected compound 11 in 57% yield. Decasaccharide 12 was then subject to palladium catalysed hydrogenolysis, to remove benzyl protecting groups and reduce the linker azido group to an amine, using our developed optimized conditions, yielding 13 after P-2 size exclusion chromatography (Scheme 1B) (28,32).…”

Section: Design and Synthesis Of Fret Probesmentioning

confidence: 99%

A glycan FRET assay for detection and characterization of catalytic antibodies to theCryptococcus neoformanscapsule

Crawford

Wear

Smith

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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Classic antibody functions include opsonization, complement activation, and enhancement of cellular antimicrobial function. Antibodies can also have catalytic activity, although the contribution of catalysis to their biological functions has been more difficult to establish. With the ubiquity of catalytic antibodies against glycans virtually unknown, we sought to advance this knowledge. The use of a glycan microarray allowed epitope mapping of several monoclonal antibodies (mAbs) against the capsule of Cryptococcus neoformans. From this, we designed and synthesized two glycan-based FRET probes, which we used to discover antibodies with innate glycosidase activity and analyze their enzyme kinetics, including mAb 2H1, the most efficient identified to date. The validity of the FRET assay was confirmed by demonstrating that the mAbs mediate glycosidase activity on intact cryptococcal capsules, as observed by a reduction in capsule diameter. Furthermore, the mAb 18B7, a glycosidase hydrolase, resulted in the appearance of reducing ends in the capsule as labeled by a hydroxylamine-armed fluorescent (HAAF) probe. Finally, we demonstrate that exposing C. neoformans cells to catalytic antibodies results in changes in complement deposition and increased phagocytosis by macrophages, suggesting that the antiphagocytic properties of the capsule have been impaired. Our results raise questions over the ubiquity of antibodies with catalytic activity against glycans and establish the utility of glycan-based FRET and HAAF probes as tools for investigating this activity.

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Section: Design and Synthesis Of Fret Probesmentioning

confidence: 99%