RT Journal Article SR Electronic(1) A1 Payne, J. W.YR 1974 T1 Peptide Transport in Escherichia coli: Permease Specificity towards Terminal Amino Group Substituents JF Microbiology, VO 80 IS 1 SP 269 OP 276 DO https://doi.org/10.1099/00221287-80-1-269 PB Microbiology Society, SN 1465-2080, AB 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., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-80-1-269