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Constrained Peptide Library Construction

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Constrained Peptide Library ConstructionCreative Biolabs developed a constrained peptide library construction technology, which offers constrained peptides with target-adapted cross-links. Our technology involves generating natural or semi-synthetic peptides with constrained structures to retain and improve the properties (e.g. stability, resistance to protease activity, protein binding affinity, intrinsic cell permeability, etc.) of the peptides. Our platform has been optimized over the years to include Positional Stabilization Method, Positional Cyclization Method and Phage Display Peptide Library Method.

Positional Stabilization Method

Constrained Peptide Library ConstructionCreative Biolabs has developed a broadly applicable technology for “freezing” the 3D-structure of short peptides (20-30 amino acids) using a small rigid entity that carries 2~4 anchor points as a scaffold. The peptide slowly adopts a well-defined three-dimensional structure around the scaffold and loses flexibility with the scaffold entity in the center, forming not limited to single loop peptide without fully aqueous conditions at neutral pH. This platform technology not only rigidifies the structure of the peptide but also improves its binding activity and proteolytic stability.

Positional Cyclization Method

Constrained Peptide Library ConstructionPositional Cyclization Method is another new peptide conformation stabilizing technology. This technique involves synthesis of peptides with constrained structures in the form of lactam bridge or disulfide bond and stapling at various positions to fix the overall structure conformation of the protein. This technology not only offers peptides with desirable pharmacokinetic properties but also retains the sequence flexibility that permits the introduction of new and diverse functionalities.

Phage Display Peptide Library

Constrained Peptide Library ConstructionWe have nature monomeric proteins as scaffolds displayed on the surface of filamentous bacteriophage M13 with one or more loops of the scaffold framework randomized using PCR mutagenesis as a constrained random peptide library. We have also constructed random nonapeptide libraries in the N-terminal region of the coat protein of bacteriophage with lactam bridge or disulfide bond flanking the insert. All these constrained peptide libraries represent structural diversity and biochemical stability intended for therapeutic use.

We are professional in providing constrained peptides of extremely high diversity and specificity. Our drug-like peptides are highly stable and of chemical structures that offer extremely high intrinsic cell permeability.




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