Peptides design

In light of the importance of the / -turn motif in peptide and protein recognition, and the design and synthesis of bioactive small molecules, / -turn mimetics has attracted considerable attention. Seebach and coworkers have shown recently that low molecular weight open-chain / - and y-peptides designed to promote turn formation can be used as templates for mimicking the a-peptide hormone somatostatin. 

Rajagopal K, Ozbas B, Pochan DJ et al (2005) Self-assembled hydrogels from beta- hairpin peptides tuning responsiveness and bulk material properties by peptide design. Biopolymers 80 487 87... 

Haines-Butterick L, Rajagopal K, Branco M et al (2007) Controlling hydrogelation kinetics by peptide design for three-dimensional encapsulation and injectable delivery of cells. Proc Natl Acad Sci 104 7791-7796... 

Constrained -amino acids, which have gained widespread use in peptide design and are important for controlling secondary structures, were prepared by Kotha and colleagues76 via Diels-Alder reactions of outerring diene 56 with several dienophiles, followed by... 

This designed construct, as such, may not influence subsequent steps of transamination due to loss of the strong association between the coenzyme and the synthetic peptide after amino acid binding. However, the selectivity of the peptide for pyridoxal phosphate reveals the potential power of peptide design and the importance of secondary binding interactions for defining the formation of specific binary complexes. 

In the S-peptide design, the Pal residue was introduced at position 8, replacing the native phenylalanine (Fig. 9) [22]. Lysine residues, which have the potential to form Schiff bases with the pyridoxal functionahty, and a potentially oxidatively unstable methionine residue were replaced with either norleucine or glycine. These changes resulted in a modified S-peptide that associated with S-protein at levels comparable to the original S-peptide. 

Gleason and Kazlauskas have introduced the concept of pseudodynamic combinatorial chemistry [38,39], which combines an irreversible synthesis of library components with an irreversible destruction step. The idea is illustrated in Scheme 2.8 for a pseudo-DCL of peptides designed to inhibit... 

Chen, H. M., Muramoto, K., Yamauchi, F., Fujimoto, K., and Nokihara, K. (1998). Antiox-idative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. J. Agric. Food Chem. 46, 49-53. 

Coil-Ser A Peptide Designed as Parallel Homodimer that Forms an Up-Up-Down Homotrimer (1990)... 

Harbury et al. (1998) described a series of peptides designed to form dimeric, trimeric, and tetrameric helical bundles with right-handed supercoils. To achieve right-handed coiled coils, rather than canonical left-handed structures, an HP pattern based on an 11-residue abcdefghij repeat was used as a template. Combinations of the hydrophobic residues Ala, lie, Leu, Val, allo-Ile, and nor-Val were considered for the a, d, and h sites. The... 

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