Study of peptide–sugar non‐covalent complexes by infrared atmospheric pressure matrix‐assisted laser desorption/ionization

Abstract

Infrared atmospheric pressure matrix-assisted laser desorption/ionization quadrupole ion trap mass spectrometry was applied to the study of siglec binding to oligosaccharide ligands. Peptides were designed to mimic the binding sites of three members of the siglec family: sialoadhesin, MAG and CD22. These peptides were tested for their ability to complex with their carbohydrate ligands 3'-sialyllactose (3'SL) and 6'-sialyllactose (6'SL). All peptides demonstrated the ability to bind to the carbohydrates, with the peptide representing sialoadhesin maintaining its binding specificity for 3'SL in preference to 6'SL. This technique can be used to study other protein-sugar interactions and can be expanded to create high-throughput screening techniques.

On the mechanism of ion formation from the aqueous solutions irradiated with 3 µm IR laser pulses under atmospheric pressure

“…Water or glycerol alone does not provide an optimal matrix from the point of view of sensitivity and convenience. Instead, water/glycerol mixtures of different composition were used in subsequent studies 2–4. To find out the best matrix composition, a dependence of analyte peak intensity was measured against the percentage of glycerol in matrix solution.…”

“…Although few labs in the world are equipped with AP IR matrix‐assisted laser desorption ionization (MALDI) sources, the technique was recently successfully applied for MS analysis of oligosaccharides 2–4. The understanding of the mechanism of ion production is important for the application and optimization of any technique.…”

Biologically-Inspired Peptide Reagents for Enhancing IMS-MS Analysis of Carbohydrates

“…A recent report suggests that peptide-carbohydrate interactions are capable of distinguishing between different anomeric forms of a saccharide molecule [23]. We also note the related work by Cotter and Von Seggern utilizing biologically-relevant interactions between peptides and carbohydrates in mass spectrometry experiments [24,25].…”

Super-resolution imaging in glycoscience: New developments and challenges

“…75 The engineered peptides can be designed and synthesized from the crystal structure of toxins or lectins, such as, the peptide from pertussis toxin can bind to sialylated conjugates, 76 the one from E-selectin was identi¯ed to bind to SLe X;77 , and the one was designed to mimic the binding sites of siglec family. 78 Additionally, novel carbohydrate-binding peptides were acquired by phage-display technology (a phage display approach followed by biopanning), including the peptide against T antigen (Gal1-3 GalNAc), 79 the ones against sialylated, 80 and sulfated Lewis antigens. 81 With the development of high-throughput assays and cost-e±cient chemical synthesis of peptides, random sequence peptide arrays containing 1000 peptides were used with luminescent glyconanoparticles to identify two sets of peptides that can bind to 3 0 -sialylactose and 6 0 -sialylactose.…”