Novel DARPin Library Generation with Reduced Hydrophobicity

Based on our advanced platform and extensive experience, Creative Biolabs is now offering specific custom scaffold library construction service for the novel designed ankyrin repeat proteins (DARPin) with reduced hydrophobicity.

Introduction of Designed Ankyrin Repeat Proteins (DARPin)

Ankyrin repeat protein is one of the most common binding proteins with varies functions like receptor binding and cell signaling. The basic structure of ankyrin repeat proteins can be composed with a β-turn followed by two antiparallel α-helices and a loop connected to the β-turn of the next repeat. DARPin is one of the most common protein-protein interaction motifs which also represent a typical modular approach for the library construction. With a series of advantages, now DARPins is considered to play an important role in the discovery and development of drug therapy. In general, the DARPin usually can be composed of two or three repeats based on the artificial consensus sequence. The conserved residues can be defined as invariant framework residues as for each repeat and there are six variable amino acid positions available for the randomization.

Construction of Novel Designed Ankyrin Repeat Proteins (DARPin) Library

Currently, scientists from Creative Biolabs can offer a novel DARPin library construction strategy. Compared with the original DARPin based on the consensus design approach, such novel DARPin endows multiple special features such as reduced hydrophobicity. For the randomized positions, the novel DARPin limits the number of permitted residues to generate more hydrophilic DARPins and reduce the unspecific hydrophobic interactions. For the capping repeats, we choose to use smaller residues to replace the N-cap but not to randomize it. In this case, the sterical interference with DARPin binding would be reduced. The C-cap of original library is the least stable repeat of DARPins, now we found an improved sequence that the amino acid compositions which are identical to the ones of the internal repeats can randomize the β-turn of the C-cap.

Randomization of the internal DARPin repeat. (Seeger, M.A.; et al 2013)Fig.1 Randomization of the internal DARPin repeat. (Seeger, M.A.; et al 2013)

Features of the novel DARPins:

Creative Biolabs is one of the well-recognized experts who are professional in applying advanced phage display technologies for a broad range of project objectives and we can also offer varies of scaffold protein library construction services. We are pleased to use our extensive experience and advanced platform to offer the best service and the most qualified products to satisfy each demand from our customers. If you are interested in our novel DARPin library construction service, please do not hesitate to inquire us for more details.


  1. Seeger, M.A.; et al. Design, construction, and characterization of a second-generation DARPin library with reduced hydrophobicity. Protein Science. 2013, 22(9):1239.

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