ArticleACS applied bio materials2026
AFM-Based Single-Molecule Force Spectroscopy of PEG-Anti-PEG Antibody Interactions.
Article in ACS applied bio materials, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Pressure-Dependent Diffusion of PEG-Functionalized Gold Nanoparticles Probed by X-ray Photon Correlation Spectroscopy.The journal of physical chemistry. B · 2026Article
- In-Depth Characterization of PEGylated Liposomes: Using AF4 and HPLC-CAD in Tandem as a Strategy for Composition Assessment and Postinsertion Optimization.Analytical chemistry · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poly(ethylene glycol) (PEG) is widely used as a stealth polymer to enhance drug stability and circulation by reducing immune recognition. However, anti-PEG antibodies are increasingly reported in humans, leading to accelerated drug clearance and adverse immune responses. While ensemble assays have clarified the scheme of PEG-antibody binding, they lack the resolution to probe molecular-scale mechanics. Here, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to examine how PEG terminal chemistry and antibody maturation modulate these interactions. Methoxy- (m-PEG) and hydroxy-terminated PEG (HO-PEG) were tested against Fv-clasps from two anti-PEG IgMs: the naïve IgM M9 and the affinity-matured IgM M11. M11 bound PEG more strongly and at shorter rupture distances than M9, with 2D force-distance maps revealing the most intense signatures for M11 and m-PEG pair. Complementary quartz crystal microbalance with dissipation (QCM-D) and Fourier-transform infrared (FTIR) spectroscopy confirmed higher binding by M11 and a terminal preference of M9 for m-PEG. In addition to antibody maturation, we report that the hydrated structure of PEG plays a significant role in PEG-antibody binding. HO-PEG forms extended, hydrated layers, whereas m-PEG adopts compact, collapsed conformations, shaping antibody accessibility and binding mechanics. These results provide molecular-level insight into how antibody structure and PEG hydration state dictate binding, offering design principles for PEGylated therapeutics with reduced immunogenicity and improved performance.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.