The synthesis of peptides related to gramicidin S and the significance of optical configuration in antibiotic peptides. 1. Tripeptides
- 1 February 1950
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 46 (2) , 196-199
- https://doi.org/10.1042/bj0460196
Abstract
Dipeptides and tripeptides containing D-phenylalanine have been synthesized and compared as growth inhibitors with optically isomeric peptides containing L-phenylalanine. The amino-acids in these peptides were arranged in the same sequence as in gramicidin S. Limited antibiotic activity was observed with synthetic peptides, but no difference in activity was found between a tripeptide containing D-phenylalanine and bne containing L-phenylalanine. The significance of these results in relation to the origin of antibiotic activity in peptides is discussed.This publication has 8 references indexed in Scilit:
- Lysine analogues as inhibitors of bacterial growthBiochemical Journal, 1950
- A Peptide Derivative Related to GramicidinJournal of the American Chemical Society, 1948
- THE NATURE OF BACITRACIN1948
- The synthesis of some dipeptides related to gramicidin SBiochemical Journal, 1948
- Gramicidin S: the sequence of the amino-acid residues.1947
- Synthetic PenicillinScience, 1946
- ‘Gramicidin S’: over-all chemical characteristics and amino-acid compositionBiochemical Journal, 1945
- The amino-acid composition of tyrocidineBiochemical Journal, 1943