Antibiotisch wirksame Tripeptide der Sequenzl-Arg-d-X-l-Phe

Abstract

Five tripeptides with the sequence L-Arg-D-X-L-Phe showed antibiotic activity on fungi and on some pathogenic moulds. The action of the peptides could be neutralized in the cross-strip test by the L-amino acid corresponding to the D-amino acid in the middle position.

Antibiotically active tripeptides with the sequence L‐arginine—N‐α‐methyl‐L‐X—L‐phenylalanine

“…These facts agree with the results described by K6nig et al [1 ] for the isolated peptide (L-Arg-D-aThr-L-Phe) and with those of the synthetic peptides, where D-allo-threonine is replaced by other D-amino acids [2].…”

“…The results of the biological tests agree with those of earlier works [1,2] biological test as those with a D-amino acid in this position, the conclusion can be drawn, that a special conformation is not essential for antibiotic activity of tripeptides of general sequence L-Arg-X-DPhe.…”

“…Earlier experiments showed, that D-allo-threonine could be substituted in the above sequence by a numberof other D-amino acids without total loss of antibiotic activity [2]. It was hence of interest to find out if the replacement of D-allo-threonine by N-a-methyl-L-amino acids (which are found in some peptide antibiotics) would also lead to antibiotically active tripeptides.…”

“…It was hence of interest to find out if the replacement of D-allo-threonine by N-a-methyl-L-amino acids (which are found in some peptide antibiotics) would also lead to antibiotically active tripeptides. It was also of interest whether the action of these peptides could also be neutralized by L-amino acids as was shown [2] for the peptides with D-amino acids. These experiments should also clarify whether the conformation of these tripeptides (which is quite different from those with a middle D-amino acid) must be specific or not.…”

“…To investigate the structure-activity relationship of an antibiotically active tripeptide (the sequence of which is L-Arg-D-aThr-L-Phe) isolated by KiSnig et al [1 ], a sequence variation approach was used. Earlier experiments showed, that D-allo-threonine could be substituted in the above sequence by a numberof other D-amino acids without total loss of antibiotic activity [2]. It was hence of interest to find out if the replacement of D-allo-threonine by N-a-methyl-L-amino acids (which are found in some peptide antibiotics) would also lead to antibiotically active tripeptides.…”