Peptide studies. II. Growth-promoting activity of peptides of l-leucine and l- and d-valine for lactic acid bacteria

Shankman, S.; Higa, S.; Florsheim, H.A.; Schvo, Y.; Gold, Vicki A. M.

doi:10.1016/0003-9861(60)90405-7

Cited by 19 publications

(7 citation statements)

References 20 publications

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“…On the other hand, bacterial requirements for oligopeptides larger than a certain minimal size have been demonstrated, as has an apparently absolute bacterial requirement for oligopeptides (12,15,36). The demonstration of lower size limits for oligopeptide utilization, the fact that such utilization may occur in the absence of the utilization of small peptides or free amino acids, and the fact that the ability of bacteria to utilize small peptides does not ensure their ability to utilize large peptides (13,23,31) raises the question of whether or not there is a real difference in the means of bacterial utilization of large peptides as opposed to small peptides and free amino acids.…”

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confidence: 99%

Oligopeptide Uptake by Bacteroides ruminicola

1967

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Bacteroides ruminicola did not take up 14C from exogenous "C-labeled L-proline or 14C-labeled L-glutamic acid and took up very little 14C from exogenous 4C-labeled L-valine. Growing cultures of B. ruminicola rapidly took up 14C from "4C-prolinelabeled peptides of molecular weights up to 2,000 and incorporated it into trichloroacetic acid-insoluble cell material. Uptake and incorporation did not occur at 0 C and were reduced or eliminated in glucose-starved cells, depending upon the length of time the cells were starved. The initial rate of uptake of peptides seemed to exhibit saturation kinetics, but it was impossible to establish this conclusively. The initial uptake of 14C from peptides was not affected by chloramphenicol but the incorporation of it into trichloroacetic acid-insoluble cell material was virtually eliminated. Only moderate amounts of trichloroacetic acid-extractable, labeled material were present in cells during peptide uptake, whether or not chloramphenicol was present. "4C-proline was rapidly released from labeled peptides during uptake, whether or not chloramphenicol was present. The amount of "IC fixed into trichloroacetic acid-insoluble cell material was directly related to the size of peptides originally supplied in the medium. It is concluded that B. ruminicola possesses a general system for the uptake of peptides, that peptides are rapidly hydrolyzed during or after uptake, and that oligopeptides function only to supply amino acids in a form available to the organism.

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confidence: 99%

Oligopeptide Uptake by Bacteroides ruminicola

1967

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“…It has become clear from our investigations (1,3,4) and from the work of others (8)(9)(10)(11)(12)) that active transport of peptides into bacteria varies greatly with the organism and the composition of the peptides. This largely accounts for the differences in potency observed with phosphonopeptides.…”

Section: Discussionmentioning

confidence: 69%

Phosphonopeptide antibacterial agents related to alafosfalin: design, synthesis, and structure-activity relationships

Atherton¹,

Hall²,

Hassall³

et al. 1980

Antimicrob Agents Chemother

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Dipeptide variants of alafosfalin (L-alanyl-L-1-aminoethylphosphonic acid) with substantial differences in potency and antibacterial spectrum in vitro and in vivo have been synthesized. Certain dipeptides with alternptives to the L-alanyl residue had broader antibacterial spectra; activity against Pseudomonas aeruginosa was included. Some compounds had better in vivo activity than alafosfalin when introduced into infected rodents orally, but for the majority of the more active phosphonodipeptides, parenteral administration was more effective. Certain oligopeptides derived from the more active phosphonodipeptides possessed good in vitro activity against an extended range of organisms; they included Haemophilus influenzae, Streptococcus faecalis, and Streptococcus pneumoniae. The in vivo activity of some of these phosphono-oligopeptides was significantly greater than that of the parent dipeptide and correlated well with the in vitro results. This indicates that phosphono-oligopeptides exert part of their in vivo action directly, in addition to that arising from smaller peptides produced by peptidase cleavage.Phosphonopeptides constitute a class of synthetic antibacterial peptide mimetics in which the C-terminal carboxyl group has been replaced by a phosphoryl [P(O) (OH)2] function (1). These compounds are transported into bacteria by means of peptide permeases located in the bacterial cytoplasmic membrane. Within the cell they are cleaved enzymatically to liberate an aminoalkylphosphonic acid moiety which inhibits cell wall biosynthesis (3). In a previous study, phosphonopeptides containing L-amino acids linked to the L-1-aminoethylphosphonic acid Ala(P) [or less significantly, to aminomethylphosphonic acid, Gly(P)] as the acid terminal substituent were shown to forin the most interesting series of compounds (4). On the basis of antibacterial activity in vitro and in vivo and stability to mammalian peptide hydrolase enzymes, alafosfalin [L-alanyl-L-1-aminoethylphosphonic acid; Ala-Ala(P)] was selected for detailed evaluation (1-4). (All amino acids and amino acid mimetics in this paper are of the L series, and L-is therefore omitted in abbreviations.)Although alafosfalin had high levels of activity against certain members of the Enterobacteriaceae, including Enterobacter sp., Escherichia coli, Klebsiella sp., and Shigella sp., the antibacterial activity against Proteus and Pseudomonas spp. or streptococci (with the exception of Streptococcus faecalis) was modest (1, 2, 4). However, as the investigation of the mechanism of action of this new class of antibacterial agents developed, it appeared likely that phosphonopeptides with advantages over alafosfalin might be identified. This has been confirmed.In our preliminary studies (4) we observed that certain phosphonodipeptides with different natural amino acids combined with Ala(P) showed very substantial differences in antibacterial activity. A detailed investigation of L-methionyl (Met)-Ala(P) established that the enhanced activity and broader antibacterial spectrum...

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“…The observation ( Table 4) that activity was restricted to the LL series [including LAla-Gly(P)] suggested that transport into the bacterial cell utilizing an LL-dipeptide permease system (17,18,25,26) might be involved in the mechanism of action. This was supported by the finding that the antibacterial activity and transport was antagonized by LL-alanyl-alanine (4) and by evidence (Table 4) suggesting that LLbut not LD-dipeptide mimetics gave rise to intracellular 1-aminoalkylphosphonic acids, L-Ala-LAla(P) and L-Ala-Gly(P) being the most effective.…”

Section: Resultsmentioning

confidence: 99%

“…Earlier studies have shown that certain peptides, such as tri-L-ornithine (10), L-leucyl-glycine (30), D-norvalyl-D-alanine (21), and L-valyl-L-valyl-D-valine (25,26), had antimicrobial properties. Their activity seemed to depend on the action of the intact peptide on the microorganisms (20,24,28,29).…”

Section: Resultsmentioning

confidence: 99%

Phosphonopeptides as Antibacterial Agents: Rationale, Chemistry, and Structure-Activity Relationships

Atherton

Hali

Hassall

et al. 1979

Antimicrob Agents Chemother

108

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Peptide mimetics with C-terminal residues simulating natural amino acids have been designed as inhibitors of bacterial cell wall biosynthesis. The phosphonopeptide series consisting of various l and d residues of natural amino acids combined with 1-aminoalkyl (and aryl-alkyl-) phosphonic acid residues had the most interesting antibacterial properties when the C-terminal residue was l -1-aminoethylphosphonic acid. The in vitro antibacterial activities of representative phosphonodi- to phosphonohexapeptides were investigated. The antibacterial action of the active compounds has been explained in terms of transport into the bacterial cell and intracellular release of the alanine mimetic, which interferes with the biosynthesis of the peptidoglycan of the bacterial cell wall.

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Peptide studies. II. Growth-promoting activity of peptides of l-leucine and l- and d-valine for lactic acid bacteria

Cited by 19 publications

References 20 publications

Oligopeptide Uptake by Bacteroides ruminicola

Oligopeptide Uptake by Bacteroides ruminicola

Phosphonopeptide antibacterial agents related to alafosfalin: design, synthesis, and structure-activity relationships

Phosphonopeptides as Antibacterial Agents: Rationale, Chemistry, and Structure-Activity Relationships

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