Peptide hydrolysis site-selective protein cleavage

Abstract Site-selective peptide/protein degradation through chemical cleavage methods is an important modification of biologically relevant macromolecules which complements enzymatic hydrolysis. In this review, recent progress in chemical, site-selective peptide btuid cleavage is overviewed, with an emphasis oti postulated mechanisms and their implications on reactivity, selectivity, and substrate scope. 

In this chapter, we survey recent (during the past 10 years) progress in site-selective peptide/protein degradation through chemical cleavage methods that complement enzymatic hydrolysis. 

An example is the active site of chymotrypsin, a manunalian digestive enzyme responsible for the degradation of proteins in food. Chymotrypsin accomplishes the hydrolysis of peptide bonds at body temperature and at physiological pH. Recall that ordinary amide hydrolysis requires much more drastic conditions (Section 20-6). Moreover, the enzyme also recognizes specific peptide linkages that are targeted for selective cleavage, such as the carboxy end of phenylalanine residues (see Section 26-5, Table 26-2). How does it do that ... 

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