Aminosuccinyl peptides

J Martinez, M Bodanszky. Side reactions in peptide synthesis. IX. Suppression of the formation of aminosuccinyl peptides with additives. Int J Pept Prot Res 12, 277, 1978. 

Capasso S, Mattia CA, Mazzarella L, Zagari A. Conformational properties of aminosuccinyl peptides. Crystal structure and conformational analysis of tert-butyloxycarbonyl-L-aminosuccinyl-glycine methyl ester. Int. J. Pept. Protein Res. 1984 23 248-255. 

Under the influence of strong acids jS-benzyl aspartyl residues give rise to aminosuccinyl peptides... 

We must add here that steric hindrance is not necessarily harmful. As mentioned before bulkiness in the activating portion of mixed anhydrides results in more unequivocal acylation reactions. Similarly, in jff-tert.butyl esters of aspartyl residues ring-closure to aminosuccinyl peptides, observed with the corresponding )8-benzyl esters, does not occur. Furthermore, formation of hydantoins and succinimide derivatives is considerably enhanced if glycine is involved in the process, because di-acylation of this unique amino acid without a side chain readily occurs. Accordingly, it is a mistake to use glycine in model experiments designed for the study of side reactions. 

M Bodanszky, JZ Kwei. Side reactions in peptide synthesis. VI1. Sequence dependence in the formation of aminosuccinyl derivatives from P-benzyl-aspartyl peptides. 

The effect of the incorporation of a succinimide (21) moiety into a peptide chain (another type of Cj -o- Nj. ring restriction) has been examined carefully (60, 61). The five-membered succinimide annular system is an intermediate in the repair of selective degradations of side-chain deamidated proteins. It has been shown both theoretically and experimentally that L-Asu-Xxx- (Asu, a-aminosuccinyl) dipeptide sequences strongly favor the type-lT fS-tum, a behavior similar to that of the y-lactam modification discussed above. 

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See also in sourсe #XX -- [ , ]

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