According to “The Proteome Code” concept introduced by J. Biro and our early development of affinity peptide calculation method it was studied the possibility of high affinity peptide chromatographic gels development for human fibrinogen and thrombin – the basic components of the fibrin surgery glue or sealant. Given the next step of virus inactivation of fibrinogen and thrombin directly in the chromatographic column, the peptide-affinity gels had to bind these proteins at several spatially spaced points in order to limit the degree of freedom of the protein for holding proteins at high buffer flow rates or elevated buffer temperatures without denaturation. Based on previous experiments, an peptide-affinity chromatographic gelss with the following properties were developed: the dynamic binding capacity with enough residence time 20 min was around 42-54 mg×mL-1 led to the 87-92.0% purity of isolated fibrinogen and thrombin. The virus inactivation/elimination of these proteins (coupled by the gels) directly in chromatographic column shown a highly effective virus elimination (log10>9) for both nonenveloped and lipid enveloped viruses. Using fibrinogen and thrombin sequence from UniProt_KB and dates from more than 30 literature sources on the protein interaction, affinity peptides were calculated against several sequences or separate amino acids. Then these peptides were modified to reach more affinity enhancement and affinity-peptide chromatographic gels were synthetized and tested. By synthetized gels fibrinogen and thrombin, activated from prothrombin, were purified with acceptable quantity and activity.