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Abstract
SUMMARY: Escherichia coli possesses permeases that specifically transport exogenous peptides with a free or β-N-methylated terminal amino group, but not with a terminal acyl group. To determine whether steric hindrance or loss of positive charge might be responsible for inactivity of acyl peptides we prepared and tested a series of β-N -alkyl peptides, several with alkyl substituents larger than the inactivating acyl groups. β-N-dimethyl, -ethyl, -propyl, -butyl, -isopropyl and -isobutyl peptides were prepared by NaBH4 treatment of aldehyde or ketone-peptide complexes. The positively charged monoalkyl derivatives of triglycine were all nutritionally active, all competed with unsubstituted peptides, and all failed to be absorbed by a mutant that lacked the oligopeptide permease. Dimethyltriglycine was nutritionally and competitively inactive. The results negate the explanation of steric hindrance and suggest a requirement for an N-terminal β-amino hydrogen for peptide transport.
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