Lau YH, De Andrade P, Wu YT et al (2015) Peptide stapling techniques based on different macrocyclisation chemistries. Kawamoto SA, Coleska A, Ran X et al (2012) Design of triazole-stapled BCL9 alpha-helical peptides to target the beta-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction. Zhao H, Liu QS, Geng H et al (2016) Crosslinked aspartic acids as helix-nucleating templates. Tu L, Wang D, Li Z (2019) Design and synthetic strategies for helical peptides. Science 305:1466–1470Įdwards TA, Wilson AJ (2011) Helix-mediated protein-protein interactions as targets for intervention using foldamers. Walensky LD, Kung AL, Escher I et al (2004) Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix. Walensky LD, Bird GH (2014) Hydrocarbon-stapled peptides: principles, practice, and progress. Hu K, Geng H, Zhang Q et al (2016) An in-tether chiral center modulates the helicity, cell permeability, and target binding affinity of a peptide. Tsomaia N (2015) Peptide therapeutics: targeting the undruggable space. Vlieghe P, Lisowski V, Martinez J et al (2010) Synthetic therapeutic peptides: science and market. Bioorg Med Chem Lett 26:707–713Īli AM, Atmaj J, Van Oosterwijk N et al (2019) Stapled peptides inhibitors: a new window for target drug discovery. Wojcik P, Berlicki L (2016) Peptide-based inhibitors of protein-protein interactions. This chapter will systematically introduce approaches for helical stabilization of peptide macrocycles, such as ring-closing metathesis (RCM), lactamisation, cycloadditions, reversible reactions, thioether formation as well as newly found sulfonium center formation and the common use of helical stabilized macrocyclic peptides. Compared with unmodified short peptides, stable α-helix macrocyclic polypeptides have better biophysical properties including higher serum stability, cell permeability, and higher target affinity. These stable macrocyclic peptides have been applied in PPI inhibitors and self-assembly materials. These strategies can be divided into two categories: side chain to side chain cross-linking and N-terminal helix nucleation. If your printer supports automatic printing on both sides, follow these steps.Over the past two decades, significant efforts have invested in the development of strategies for the stabilization of macrocyclic peptides with α-helix structure by stapling their architectures. When you print the booklet, check the print settings to make sure you print on both sides of the paper and flip the papers correctly for the printing to work as intended. Make sure your printer is stocked with paper of the right size. Keep in mind that the final size of the booklet is one half of the paper size. Go to File > Page Setup and check the paper size. If your document already has content, the text is formatted automatically, but you might need to adjust objects like images and tables manually. For example, to add borders to every page, on the Layout tab of the Custom Margins window, select Borders. You can add many embellishments to your booklet’s appearance. To reserve space on the inside fold for binding, increase the width of the Gutter. Under Sheets per booklet, choose how many pages to print per booklet. Tip: If you have a long document, you might want to split it into multiple booklets, which you can then bind into one book. To avoid pages from printing upside down, flip the sheets on the short edge of the paper according to your printer’s instructions. If your printer doesn’t support automatic printing on both sides, select Manually Print on Both Sides, and feed the pages back to the printer when prompted. Choose the option Flip pages on short edge to avoid printing the second side of each sheet upside down. If your printer supports automatic printing on both sides, change Print One Sidedto Print on Both Sides. For example, to add borders to every page, on the Layout tab of the Page Setup window, click Borders.Ĭlick OK.

Tip: You can add many embellishments to your booklet’s appearance.

Stapled book