2 research outputs found
Dual-Functionalized Magnetic MetalāOrganic Framework for Highly Specific Enrichment of Phosphopeptides
The highly specific
enrichment of phosphoproteins and phosphopeptides
from intricate biological systems is the precondition of in-depth
phosphoproteome research. Herein, a novel dual-functionalized magnetic
zirconium-based metalāorganic framework (MOF) denoted as DFMMOF,
with the purpose of combining the affinity of immobilized metal ion
affinity chromatography (IMAC) and metal oxide affinity chromatography
(MOAC) has been successfully synthesized. The inherent ZrāO
cluster of DFMMOF particles acted as MOAC and the immobilized titaniumĀ(IV)
ions served for IMAC. The obtained DFMMOF exhibited rapid magnetic
separation (within 5 s), large surface area (237.9 m<sup>2</sup> g<sup>ā1</sup>), high binding capacity (100 mg g<sup>ā1</sup>), and good postenrichment recovery (84.8%). Thanks to the strong
affinity, low detection sensitivity (5 fmol) and high selectivity
(Ī²-casein/BSA with a molar ratio of 1:1000) for phosphopeptide
enrichment were obtained using DFMMOF as absorbent. Moreover, the
effective identification of phosphopeptides from real samples (human
serum and nonfat milk) further confirmed the immense potential of
DFMMOF as a promising candidate for the detection and extraction of
trace amounts of phosphorylated peptides in complex biosamples
Maltose-Functionalized Hydrophilic Magnetic Nanoparticles with Polymer Brushes for Highly Selective Enrichment of NāLinked Glycopeptides
Efficient enrichment glycoproteins/glycopeptides
from complex biological
solutions are very important in the biomedical sciences, in particular
biomarker research. In this work, the high hydrophilic polyethylenimine
conjugated polymaltose polymer brushes functionalized magnetic Fe<sub>3</sub>O<sub>4</sub> nanoparticles (NPs) denoted as Fe<sub>3</sub>O<sub>4</sub>āPEIāpMaltose were designed and synthesized
via a simple two-step modification. The obtained superhydrophilic
Fe<sub>3</sub>O<sub>4</sub>āPEIāpMaltose NPs displayed
outstanding advantages in the enrichment of N-linked glycopeptides,
including high selectivity (1:100, mass ratios of HRP and bovine serum
albumin (BSA) digest), low detection limit (10 fmol), large binding
capacity (200 mg/g), and high enrichment recovery (above 85%). The
above-mentioned excellent performance of novel Fe<sub>3</sub>O<sub>4</sub>āPEIāpMaltose NPs was attributed to graft of
maltose polymer brushes and efficient assembly strategy. Moreover,
Fe<sub>3</sub>O<sub>4</sub>āPEIāpMaltose NPs were further
utilized to selectively enrich glycopeptides from human renal mesangial
cell (HRMC, 200 Ī¼g) tryptic digest, and 449 N-linked glycopeptides,
representing 323 different glycoproteins and 476 glycosylation sites,
were identified. It was expected that the as-synthesized Fe<sub>3</sub>O<sub>4</sub>āPEIāpMaltose NPs, possessing excellent
performance (high binding capacity, good selectivity, low detection
limit, high enrichment recovery, and easy magnetic separation) coupled
to a facile preparation procedure, have a huge potential in N-glycosylation
proteome analysis of complex biological samples