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- W2952078220 abstract "Publisher Summary This chapter discusses the new strategies and applications made available by the establishment of peptide libraries and describes the design of the secondary structure of peptides. The introduction of peptide synthesis on solid phase dramatically increased the speed of synthesis and became an indispensable tool for the rapid production and screening of pharmacologically active analogs. The representative approaches of this new technology involve multipin peptide synthesis, one bead-one peptide approach, modified tea-bag method, and light-directed spatially addressable parallel chemical synthesis. In designing of the secondary structure of peptides, it is suggested that turns that extend over three or four amino acids and are stabilized by hydrogen bonds in proteins, can be reproduced in peptides either by introduction of pairs of proline-like constrained residues, or by the synthesis of covalently stabilized turn mimetics. Both these important secondary structural elements can be seen either as the beginning of an a-helix or P-pleated sheet or as the first step towards peptide cyclization. In addition, other applications of chemically modified peptides demonstrating again the versatility of peptides as multipurpose tools in pharmacology and biotechnology are described." @default.
- W2952078220 created "2019-06-27" @default.
- W2952078220 creator A5030697398 @default.
- W2952078220 date "1996-01-01" @default.
- W2952078220 modified "2023-10-17" @default.
- W2952078220 title "Peptides: Multiple Purpose Tools" @default.
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- W2952078220 doi "https://doi.org/10.1016/s1569-2558(08)60137-x" @default.
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