Peptides backbone modifications

Spatola, A. F., Peptide backbone modifications, in Chemistry and Biochemistry of Amino Acids. Peptides, and Proteins (B. Weinstein, ed.), Marcel Dekker, New York, 1983, pp. 268-357. 

M. Zanda, Trifluoromethyl group An effective xenobiotic function for peptide backbone modification. New J. Chem. 28 (2004) 1401-1411. http //www.nibib.nih.gov/in Vol. 2006. http //imaging.cancer.gov/in Vol. 2007. http //www.molecularimaging.org. http //www.ismrm.org/. http //interactive.snm.org/in Vol. 2007. 

In recent times peptide analogs have also been produced by a modification of the CO—NH bond (peptide backbone modification),9) ... 

The replacement of amide bonds by retro-in-verso amide replacements (71, 72) and other amide bond isosteres generates pseudopeptides (11). This process was first used to stabilize peptide hormones in vivo and later to prepare transition state analog (TSA) inhibitors. Systematic efforts to convert good in vitro inhibitors into good in vivo inhibitors became the driving force for further development of peptidomimetics. Figure 15.17 illustrates some of the peptide backbone modifications that have been made in an effort to increase bioavailability. Replacement of scissile amide (CONH) bonds with groups insensitive to hydrolysis (e.g., CHaNH) has been extensively practiced. Reviews of this work have appeared (11,73). Removal of the proton donors and... 

Zanda, M. (2004) Trifluoromethyl group an effective xenobiotic function for peptide backbone modification. New Journal of Chemistry, 28, 1401-1411. 

Table 7.2. Examples of Peptide Backbone Modifications Unit-Replacing Peptide (-CONH-) BondNomenclature Symbol...

CuAAC-Mediated Peptide Backbone Modification Strategies... 

---