Recombinant bioactive peptides

Lee, E.K. and Lee, J.D., Solid-phase, N-terminus-specific, mono-PEGylation of recombinant inter-feron-alpha-2a Purification, characterization, and bioactivity, presented atint. Symp. on the Separation of Proteins, Peptides and Polynucleotides, Aachen, Eederal Repubhc of Germany, Oct 19-22, 2004. 

By exploiting the use of recombinant DNA technology it is possible to redesign the molecular structure of rPBPs in order to combine bioactive domains and in this way achieve the creation of highly customable functionalized materials. Materials with antimicrobial properties can be obtained by fusion with antimicrobial peptides for biodefensive purposes [36]. By combining the rPBPs with UV protective peptides it is possible to create a photo-protective material for the prevention of photoaging in human skin [36]. The incorporation of cellulose binding peptides... 

Coiled coils are interesting as designable cross-linkers because of the well-understood relation between the peptide sequence, the folded and dimerized structure, and the binding affinity. However, as described above, hydrogels based on coiled coils are generally weak, with shear moduli only up to 1 kPa. Furthermore, the use of recombinant protein expression or solid-phase peptide synthesis limits the scale on which these materials can be prepared. However, this approach allows tuning both the cross-Unks as well as the backbone to regulate the mechanical properties and incorporate bioactivity. 

Along with the recent advance of recombinant DNA techniques, a wide range of bioactive molecules like proteins, peptides, and enzymes are commercially available as drugs. 

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