Block-Sequence-Specific Glycopolypeptides with Selective Lectin Binding Properties

Abstract

Glycopolypeptides with defined block sequences were prepared by sequential addition of two different N-carboxyanhydrides (NCAs), followed by selective deprotection and functionalization of pre-defined positions within the polypeptide backbone. The sequential arrangement of the galactose units and the block sequence length have been systematically varied. All the glycopolypeptides have been obtained with a similar overall composition and comparable molecular weights. Circular dichroism measurements revealed some dependence of the secondary structure on the primary composition of the glycopolypeptides at physiological pH.While statistical, diblock and tetrablock glycopolypeptides adopted random coil conformation, the octablock glycopolypeptide was mostly α-helical. The ability to selectively bind to lectins was investigated by turbidity measurements as well as Surface Plasmon Resonance (SPR) studies. 2It was found that the extent of binding was dependent on the position of the galactose units and thus the primary glycopolypeptide structure. The octablock glycopolypeptide favored interaction with lectin RCA120 while the tetrablock glycopolypeptide demonstrated the strongest binding activity to Galectin-3. The results suggest that different lectins are very sensitive to glyco coding, and that precise control of carbohydrate units in synthetic polymeric glycopeptides will remain important.

Mannose‐based graft polyesters with tunable binding affinity to concanavalin A

“…Due to the difficulty of obtaining a homogeneous form of glycoproteins, synthetic mimics of glycoproteins, such as glycopolymers, are generally utilized to study the interactions between carbohydrates and lectins . The ability of glycopolymers to interact with lectins was found to be greatly influenced by many factors, such as the rigidity of the polymer, the density of sugar molecules, polymer molecular weight and polymer architectures . For example, Kobayashi et al synthesized rigid cylindrical phenyl isocyanide glycopolymers and compared their lectin‐binding behaviour with flexible phenylacrylamide glycopolymers .…”

“…7 The ability of glycopolymers to interact with lectins was found to be greatly influenced by many factors, such as the rigidity of the polymer, the density of sugar molecules, polymer molecular weight and polymer architectures. [8][9][10][11][12] For example, Kobayashi et al…”

Synthesis and Self‐assembly of a Helical Polymer Grafted from a Foldable Polyurethane Scaffold

“…To check such possibilities, pH dependent CD spectra of PU‐PP‐1 were monitored (Figure a). At pH 10, the CD spectrum showed a maximum ellipticity at λ =218 nm and minimum ellipticity at λ =190 nm indicating random coil conformation of PU‐PP‐1 –. Whereas at pH 4.5, the polypeptide chains adopted a α‐helical conformation, as indicated by the two ellipticity minima at λ =208 and 222 nm.…”

Guided Cell Attachment via Aligned Electrospinning of Glycopolymers

“…While this capacity to control cell organization has previously been demonstrated with peptide functionalized aligned fiber polymers, this is the first time that a synthetic glycopolymer has been shown to exhibit the same effect on cell attachment. Previous studies have demonstrated that synthetic glycopolymers can interact specifically with human C‐type lectins and the sequence of sugar moieties diversifies the specific interaction, potentially explain this promising cell–material interaction. However, the mechanisms by which tenocytes interact with glycopolymers needs to be addressed by further study.…”