Systematic degradation of peptides from the carboxyl end

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Abstract
Warm methanolic hydrogen chloride and boron trifluoride in formic acid bring about N, O-acyl migration in N-glycylaminoethanol and N-L-leucylglycylaminoethanol in good yield. Alcoholysis of beta-amino esters is considerable with the former reagent and a number of secondary products not identified are formed with the latter. N, O-Acyl migration in beta-hydroxyamides derived from N-toluene-p-sulfonyl peptide esters was achieved in 85-90% yield by using phosphorus oxychloride at room temperature. The beta-amino ester hydrochlorides were isolated in crystalline form. Reductive cleavage of beta-amino esters with lithium borohydride liberated the terminal amino alcohol in 85-90% yield. The residual peptide at this stage was simultaneously converted into a new beta-hydroxyamide capable of rearrangement with phosphorus oxychloride.
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