An abnormal level of well-known his-rich protein, hemoglobin is related to various diseases. Efficient isolation of hemoglobin is of great significance in early disease diagnosis and biomedical analyses. Developing high-performance adsorption materials has become a research hotspot at present. This study proposes a facile pyrolysis-based strategy to prepare novel magnetic flower-like composites for selective hemoglobin separation. Methoxy-polyethylene glycol-carboxyl (PEG) can impart adhesion resistance to improve adsorption selectivity due to its unique ethylene oxide groups and the repulsive elastic forces from compression of the brush-like chains. Two types of magnetic composites were constructed from bimetallic metal–organic frameworks utilizing Co²⁺ and Ni²⁺ ions as magnetic sources and metal nodes, as well as modification with or without PEG. The properties of the two composites were demonstrated via FTIR, SEM, TEM, DLS, XPS, TGA, BET, and VSM analyses, including flower-like morphology, uniform size (∼2 μm), good dispersibility, porous structure, large surface area, and good magnetic responsiveness. The protein adsorption capacity was further investigated from material factor including the composites modified with/without PEG and environmental factors including incubation time, protein concentration and incubation temperature. Moreover, the adsorption behaviors were explored by kinetics and thermodynamic analysis. Both the PEG-modified and non-PEG-modified composites were effective magnetic adsorbents for selective hemoglobin separation, besides exhibited different adsorption mechanism due to introduction of PEG which induced non-spontaneous selective adsorption rather than spontaneous pure physical adsorption. The magnetic bimetallic MOF system shows promise for isolating His-rich proteins from complex biological systems.

Hymenopteran venoms contain diverse proteins and peptides that shape envenomation, defense, predation, and allergic responses. Honeybee venom from Apis mellifera is well characterized, while molecular resources for the Asian giant hornet Vespa mandarinia remain less curated. We compared protein- and peptide-fraction LC-MS/MS identification datasets from V. mandarinia venom (VM-V) and A. mellifera venom (AM-V), supported by a de novo V. mandarinia transcriptome-derived database. Protein-level identification yielded 197 protein groups in VM-V PRO and 164 protein groups in AM-V PRO. AM-V contained well-recognized honeybee venom components, including phospholipase A2, hyaluronidase, venom acid phosphatase, venom dipeptidyl peptidase 4, melittin precursor, mast cell degranulating peptide precursor, secapin, and allergen Api m 6. VM-V PRO contained transcriptome-supported candidate venom-associated proteins, including venom dipeptidyl peptidase 4-like, hyaluronidase-like, venom allergen 5-like, serine protease-like, apolipophorin-like, and hexamerin-like entries. Peptide-fraction annotation was strongest in AM-V PEP, led by melittin precursor, whereas VM-V PEP remained largely unannotated. The study focuses on identification, annotation, and hypothesis-generating functional summaries, not replicate-level differential abundance. GO, KEGG, and STRING analyses organized functional annotation patterns and prioritized candidate protein groups. These data provide an identification-based comparative venomomics resource for VM-V and AM-V and a foundation for targeted validation of candidate V. mandarinia venom-associated components.