Synthesis of silk fibroin-glycopolypeptide conjugates and their recognition with lectin.

Silk fibroin (SF), the natural fibrous protein created by the Bombyx mori silk worm, is being increasingly explored as a biomaterial for tissue engineering due to its excellent mechanical strength, high oxygen/water permeability, and biocompatibility. It is also well known that surface modification of SF with organic ligands such as the extracellular protein binding Arg-Gly-Asp (RGD) peptides help adhesion and proliferation of cells better-a key requirement for it to function as extracellular matrices. In this work, we have conjugated synthetic glycopolypeptides (GPs) that were synthesized by controlled ring-opening polymerization of α-manno-lys N-carboxyanhydrides (NCAs) onto SF by using Cu catalyzed click reaction to synthesize a new hybrid material (SF-GP), which we believe will have both the mechanical properties of native SF and the molecular recognition property of the carbohydrates in the GP. By controlling the amount of GP grafted onto SF, we have made three SF-GP conjugates that differ in their ability to assemble into films. SF-GP conjugates having a very high content of GP formed completely water-soluble brush-like polymer that displayed very high affinity toward the lectin concanavalin-A (Con-A). Films cast from SF-GP conjugates using lower amounts of grafted GP were more stable in water, and the stability can be modulated by varying the amount of GP grafted. The water-insoluble film SF-GP(25) was also found to bind to fluorescently labeled Con-A, as was seen by confocal microscopy. Such SF-GP hybrid films may be useful as mimics of extracellular matrices for tissue engineering.