{'fraction_non_alphanumeric': 0.025932953826691967, 'fraction_numerical': 0.0, 'mean_word_length': 5.731914893617021, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Temperature switchable glycopolymers and their conformation-dependent binding to receptor targets.

The temperature-dependent binding of copolymers from poly(N-isopropylacrylamide) (PNIPAM) and mannose ligands to E. coli and concanavalin A (ConA) is determined. Through polymer analogous reactions using poly(N-acryloxysuccinimide) and amine-linked mannose residues with different linkers, glycopolymers are prepared under variation of the mannose density. Quantitative adhesion-inhibition assays show the inhibitory potential of the glycopolymers as a function of the mannose/NIPAM ratio and linker type above and below their lower critical solution temperature (LCST). Intriguingly, opposite temperature effects on the binding to E. coli and ConA are observed. While the E. coli inhibition is stronger above the LCST, the ConA inhibition is overall weaker at elevated temperature. When going beyond the LCST, the polymers undergo a coil-to-globule transition, forming microphases with surface-enriched hydrophilic sugar moieties explaining increased E. coli inhibition by steric shielding. However, the formation of such microphases above the LCST renders a fraction of carbohydrate ligands inaccessibleand polymers remaining in the solution phase then have coil sizes below the minimum binding site spacing of the ConA receptor explaining reduced ConA inhibition. Overall these results suggest that the coil-to-globule transition of glycopolymers may induce lower or higher inhibitory potentials due to the adverse effects of steric shielding and carbohydrate ligand accessibly.