Serine and cysteine proteases are potently inhibited by peptide aldehydes. Compared with the plethora of methods available for solution synthesis of peptide aldehydes, there are relatively few methods for the solid phase synthesis of peptide aldehydes. The development of novel linkers for the solid phase synthesis of peptide aldehydes is reported (Scheme 1). When X = N, the aldehyde 4 can be cleaved in mild acid with 97% enantiomeric excess (e.e.). When X = O, base hydrolysis results in aldehyde 4 cleavage with complete epimerisation of the α-stereocentre. The use of Mucor meihei lipase and penicillin acylase generates the aldehyde 4 in 19 and 31% yield respectively, with complete retention of chiral integrity (>99%). The utility of linker 1 was demonstrated by the solid phase synthesis of a tetrapeptide aldehyde.