Dataset Information

IDA (Iminodiacetic Acid) Generated Mesoporous Nanopolymer - A Template to Relate Surface Area, Hydrophilicity and Glycopeptides Enrichment

ABSTRACT: Co-polymer 1,2-epoxy-5-hexene and divinyl benzene with terminal oxirane group is synthesized for the first time. High density of hydrophilic groups (-COOH, -OH) enhances hydrophilicity through facile functionalization with Diethylene Triamine (DETA) and chloroacetic acid. COOH-functionalized mesoporous polymeric beads provide high surface area and porosity, superior hydrophilicity, solvent resistance and good bio-capability for enriching N-Linked glycopeptides. Sensitivity, selectivity, reusability and batch to batch reproducibility are tested using model glycoproteins (HRP, IgG and avidin) and analyzed by MALDI-TOF-MS. Furthermore, N-glycosylation sites in N-glycopeptides of characteristic glycoproteins are identified from digested human serum.

INSTRUMENT(S): ultraflex, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Serum

SUBMITTER: Muhammad Sajid

LAB HEAD: Habtom W. Ressom

PROVIDER: PXD027783 | Pride | 2023-07-20

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20210727_Serumglyco_05.msf	Msf
	20210727_Serumglyco_05.raw	Raw

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Publications

Iminodiacetic acid (IDA)-generated mesoporous nanopolymer: a template to relate surface area, hydrophilicity, and glycopeptides enrichment.

Sajid Muhammad Salman MS Saleem Shafaq S Jabeen Fahmida F Fatima Batool B Zulfikar M M Ashiq Muhammad Naeem MN Ressom Habtom W HW Pukala Tara Louise TL Najam-Ul-Haq Muhammad M

Mikrochimica acta 20211111 12

A three-step strategy is introduced to develop inherent iminodiacetic (IDA)-functionalized nanopolymer. SEM micrographs show homogenous spherical beads with a particle size of 500 nm. Further modification to COOH-functionalized 1,2-epoxy-5-hexene/DVB mesoporous nanopolymer enriches glycopeptides via hydrophilic interactions followed by their MS determination. Significantly high BET surface area 433.4336 m<sup>2</sup> g<sup>-1</sup> contributes to the improved surface hydrophilicity which is also ...[more]

PMID: 34762162

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Project description:Large-scale identification of N-linked intact glycopeptides by liquid chromatography coupled tandem mass spectrometry (LC-MS/MS) in human serum is challenging due to the wide dynamic range of serum protein abundances, the lack of a complete serum N-Glycan database and the existence of non-specifically digested peptides and numerous modifications. In this regard, a spectral library search method was presented for serum N-linked intact glycopeptides identification with target-decoy and motif-specific false discovery rate (FDR) control. Low-abundant glycoproteins were firstly separated from high-abundant proteins by acetonitrile (ACN) precipitation. After digestion, the N-linked intact glycopeptides were enriched by hydrophilic interaction liquid chromatography (HILIC) column and a portion of the enriched N-linked intact glycopeptides were processed by N-Glycosidase F (PNGase F) to generate de-glycopeptides. Both N-linked intact glycopeptides and de-glycopeptides were analyzed by LC-MS/MS. From N-linked de-glycopeptides datasets, 764 N-linked glycoproteins, 1,699 N-linked glycosites and 3,328 unique N-linked de-glycopeptides were identified. The spectra of these N-linked de-glycopeptides were utilized for N-linked de-glycopeptides library construction and identification of N-linked intact glycopeptides. Four types of N-linked glycosylation motifs (NXS/T/C/V, X≠P) were used to recognize the N-linked de-glycopeptides, and two different N-Glycan mass databases including 27 modified N-Glycan masses and 712 unmodified N-Glycan masses were combined and utilized during spectral library search for identification of N-linked intact glycopeptides. In total, from the N-linked intact glycopeptides datasets, 526 N-linked glycoproteins, 1,036 N-linked glycosites, 22,677 N-linked intact glycopeptides and 738 N-Glycan masses were identified under 1% FDR, representing the most in-depth serum N-glycoproteome identified by LC-MS/MS at N-linked intact glycopeptide level and N-linked de-glycopeptides level.