Protein cages are spherical hollow macromolecules that are attractive platforms for the construction of nanoscale cargo delivery vehicles. Human heavy-chain ferritin (HHFn) is modified genetically to control the number and position of functional groups per cage. 24 β-CDs are conjugated precisely to the modified HHFn in specific locations through thiol-maleimide Michael-type addition followed by copper(I)-catalyzed azide/alkyne cycloaddition (CuAAC). The resulting human ferritins displaying β-CDs (β-CD-C90 HHFn) can form inclusion complexes with FITC-AD, which can slowly release the guest molecule reversibly in a buffer solution via non-covalent β-CD/AD interactions. β-CD-C90 HHFn can potentially be used as delivery vehicles for insoluble drugs.
Succinoglycan, a shinorhizobial exopolysaccharide produced by Shinorhizobium meliloti, is composed of an octasaccharide subunit. S. meliloti produces both high-molecular-weight and low-molecular-weight (M(r)<10 000) succinoglycans that consisted of monomer, dimer, or trimer of an octasaccharide unit. We isolated and purified the monomer among low-molecular-weight succinoglycans and used this microbial linear octasaccharide as a novel chiral additive for enantiomeric separation of some flavanones such as homoeriodictyol, hesperetin, naringenin, and isosakuranetin in CE. Throughout the present investigation, we firstly used noncyclic oligosaccharides for the chiral separation of flavanones. We also found that successful enantioseparation of four flavanones depends on the presence of succinate substituents of the linear monomeric octasaccharide in CE, suggesting that succinylation of succinoglycan monomer is decisive for the effective enantiomeric separation.
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