Molecular peptide recognition

Doyle, D. A., Lee, A., Lewis, J., Kim, E., Sheng, M., and MacKinnon, R. Crystal structures of a complexed and peptide-free membrane protein-binding domain Molecular basis of peptide recognition by PDZ. Cell 1996, 85, 1067-1076. 

In the context of this book, the term bioactivity is mainly applied to polymers that incorporate elements capable of molecular biological recognition, such as peptide sequences serving as cell adhesion ligands and polyanionic sites that utilize electrostatic interactions for the biomimetic presentation of... 

Yoshikawa and coworkers [17-22,24,26-28] were using specifically synthesized polystyrene resins with peptide recognition groups, in ablend with a matrix polymer, for the membrane formation via a dry PI process. The resulting membranes seemed to be microporous. The permeability was much higher for the MIP as compared with the blank membranes hence, the low-molecular weight templates seemed to act also as a pore former. 

EMPl, selected by phage display from random peptide libraries, demonstrates that a dimer of a 20-residue peptide can mimic the function of a monomeric 166-residue protein. In contrast to the minimized Z domain, this selected peptide shares neither the sequence nor the structure of the natural hormone. Thus, there can be a number of ways to solve a molecular recognition problem, and combinatorial methods such as phage display allow us to sort through a multitude of structural scaffolds to discover novel solutions. 

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. 

Van Regenmortel, M. H. V. (1999c), Molecular design versus empirical discovery in peptide-based vaccines. Coming to terms with fuzzy recognition sites and ill-defined structure-function relationships in immunology , Vaccine, 18, 216-221. 

Molecular determinants of recognition for the intestinal peptide carrier, J. Pharm. Sci. 1997, 86, 596-602. 

Kieffer BL. Recent advances in molecular recognition and signal transduction of active peptides receptors for opioid peptides. Cell Mol Neurobiol 1995 15 615— 635. 

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