Fibrinogen nanofibril growth and self-assembly on Au (1,1,1) surface in the absence of thrombin.

Fibrinogen (fg) molecules were observed to form very well organized patterns of nanofibrils by self-assembling on Au (1,1,1) surface without any addition of thrombin, growing in two orientations (longitude and transverse). This observation is new and unique for gold surfaces, in contrast with Mica or HOPG surfaces. Based on the experimental results, we proposed an assembly mechanism: Au-S interactions and its activated interactions in the ‘αC-domain’ are two main causes for the patterned assembly on Au(1,1,1) surface, and ‘D: D’ and ‘γXL’ interactions help the elongation and strengthening of the fibril assembly.