Abstract
RGD (Arg-Gly-Asp) peptide was identified as the minimal active core peptide sequence common to adhesive proteins. In this paper, we report preparation of RGD-albumin conjugate (RGD-ALB) and its cellular adhesive functions in vitro. RGD-ALB was prepared via coupling reaction of albumin with pentapeptide (GRGDS; Gly-RGD-Ser) by water soluble carbodiimide. Bovine endothelial cells (ECs) adhered and spread on surface coated with RGD-ALB, whereas few EC adhered on surfaces coated with GRGESP-albumin conjugate (GRGESP peptide with little cell-attachment activity; false control) and albumin. Cellular behaviors, such as adhesion, spreading, growth and migration, on surfaces coated with RGD-ALB, fibronectin (FN) and vitronectin (VN) were examined. Adhered cell number on RGD-ALB coated surface was larger than those of FN and VN. Cell morphology on RGD-ALB coated surface was similar to that on FN. The cell growth and migration activity on RGD-ALB coated surface were almost equal to those on FN and VN. Thus, RGD-ALB was found to promote cell adhesion, migration and growth as effective as fibronectin.
