Modified proteins comprising a bioactive peptide/protein linked to a sequence of aminoacids containing a human carbohydrate binding module (CBM), and development of a system for the administration of therapeutically active proteins and respective utilizations for biomedical purposes

Abstract

It has been developed a strategy to simultaneously improve the properties of starch-based biomaterials for biomedical applications and the efficiency of therapeutical proteins. This new strategy which is revealed in this invention consists of the fusion of a carbohydrate binding module (CBM) with bioactive peptides. The human CBM used in this work has starch affinity (SBM). This SBM was identified as a module of a laforin enzyme, a phosphatase, which has the function to attribute glycogen affinity. As has been demonstrated the SBM does also have starch affinity. This is a low cost polysaccharide available in large quantities and with different properties which has increasingly raised interest for the development of biomedical applications. The biocompatibility, versatility and biodegradability are relevant starch characteristics for the development of applications as the controlled release of drugs and tissue engineering.