Knowledge-based Novel Folds Design

To accurately design the fold of engineered proteins still remains a challenge. A variety of approaches for designing novel protein structures have been developed in recent years: from modification of the existing natural domains to more advanced strategies that employ computational tools and are able to design proteins from scratch. As a world-class provider of biotechnology, Creative Biolabs provides omnidirectional technologies to meet the diverse needs of our customers. With our professional experience and advanced protein engineering platform, we are confident in offering a variety of novel folds design services to meet the diverse needs of our customers.

Introduction to Novel Folds Design

The construction of complex protein folds relies on the precise conversion of a linear polypeptide chain into a compact three-dimensional structure. Examination of protein three-dimensional structures suggests that complex tertiary folds and quaternary associations can be deconstructed into a limited number of secondary structural elements, such as strands, helices, and turns, which are assembled using loosely structured loops. The primary method of many folding design strategies is the use of amino acid propensities to adopt various secondary structures. The inherent property of such a derived set of amino acids is then arranged to maximize hydrophobic interactions to form a compact core, and patterns of ionic interactions and hydrogen bonds are utilized to further stabilize the structure. An alternate approach to the design of rigid secondary structures is to exploit the constraints imposed by backbone conformations. Such a strategy dictates the use of amino acids with restricted access to conformational space such as R-aminoisobutyric acid and its higher homologs, proline enantiomers, and a variety of synthetically designed residues.

Fig.1 Various folds observed in protein structures.

Services

The design of folded polypeptide structures from ‘first principles' provides a stern test of our understanding of the principles of polypeptide chain folding. The approaches to the design of secondary structures have been proved to be fruitful. We can provide the following two novel folds design services to meet customers' specific requirements.

Design of α-peptides with non-native amino acid units

The introduction of non-peptidic units into a native peptide chain is mostly applied as turn-mimics. Turns reverse the direction of peptide helices and strands to form compact structures. They serve as epitopes in peptides and proteins. Both cyclic structures and acyclic structures were exploited to mimic turns, with conformational constraint as the key requirement. Non-native structures can also be incorporated into peptides to endow peptides with certain natural or non-natural structures and properties. For example, non-natural units can mimic a cis peptide bond, which normally requires a proline in natural peptides.

Design of β-peptides and its analogs

β-amino acids are similar to α-amino acids in which they contain an N-terminus amino group and a C-terminus carboxyl group. β-peptides are composed of β-amino acids which can exist as R or S isomers at either the α-carbon (C2) or the β-carbon (C3). The vast range of stereo- and regioisomers significantly expand the structural diversity of β-peptides. One outstanding feature of β-peptide is its helix formation manner, which is similar to that of α-peptides. Turn structures can also be mimicked in β-peptides by the introduction of a non-amino acid unit into a β-peptide sequence.

Creative Biolabs has been involved in the field of protein engineering for many years and we are fully committed to working with you to facilitate the successful completion of the projects. We have accumulated a wealth of experience from the accomplished projects and are very proud of our high-quality platforms to meet diverse needs from our clients. If you are interested in our services, please contact us for more details.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

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