Interaction of Linear Polyelectrolytes with Proteins: Role of Specific Charge-Charge Interaction and Ionic Strength.

We present a thermodynamic study of the interaction of synthetic, linear polyelectrolytes with bovine serum albumin (BSA). All polyelectrolytes are based on poly(allyl glycidyl ether) which has been modified by polymer-analogous reaction with anionic (-SONa), cationic (-NHCl or -NHMeCl) or zwitterionic groups (-NMe(CH)SO). While the anionic polymer shows a very weak interaction, the zwitterionic polymer exhibits no interaction with BSA (pI = 4.

Architectured helically coiled scaffolds from elastomeric poly(butylene succinate) (PBS) copolyester via wet electrospinning.

Electrospinning is one of the most investigated methods used to produce polymeric fiber scaffolds that mimic the morphology of native extracellular matrix. These structures have been extensively studied in the context of scaffolds for tissue regeneration. However, the compactness of materials obtained by traditional electrospinning, collected as two-dimensional non-woven scaffolds, can limit cell infiltration and tissue ingrowth.