On the mode of action of a peptide inhibitor of growth in P. cerevisiae

Shankman, S.; Gold, Vicki A. M.; Higa, S.; Squires, Richard F.

doi:10.1016/0006-291x(62)90081-5

Cited by 18 publications

(4 citation statements)

References 11 publications

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“…In contrast, the oligopeptide transport system does not require a free carboxy terminus, but the system has a reduced affinity for peptides in which the terminal carboxyl group has been modified or deleted (Payne & Gilvarg, 1968a). Growth studies, primarily with Lactobacilli (Shankman et al, 1960(Shankman et al, , 1962, have been interpreted (Payne & Gilvarg, 1971) to show that the first two N-terminal residues of an oligopeptide must be L-amino acids and that D-amino acids can be tolerated in the third (or, presumably, a subsequent) residue. Size restriction by the oligopeptide transport system depends not on the number of amino acid residues, but on the total hydrodynamic volume of the peptide (Payne & Gilvarg, 1968b).…”

mentioning

confidence: 99%

Photoaffinity inhibition of dipeptide transport in Escherichia coli

Staros¹,

Knowles²

1978

Biochemistry

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A dipeptide containing a nitrene precursor, glycyl-4-azido-2-nitro-L-phenylalanine, has been synthesized. This compound is a photoaffinity inhibitor of dipeptide transport in E. coli. In the dark, the dipeptide is a reversible inhibitor of glycylglycine uptake by live E. coli W cells. The 14C-labeled compound is a substrate for the transport system, with a Km of 7 micrometer and V max of 5 x 10(3) molecules cell-1 s-1 (compare 9 micrometer and 1 x 10(4) molecules cell-1 s-1, respectively, for the transport of glycylglycine under the same conditions). When intact E. coli cells are photolyzed at approximately 350 nm in the presence of the photolabile dipeptide, their ability to transport either glycylglycine or unphotolyzed glycyl-4-azido-2-nitro-L-phenylalanine is irreversibly inhibited, but their ability to transport arginine is unaffected. The presence of glycylglycine in the medium during photolysis protects the cells against the light-dependent inactivation of dipeptide transport.

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confidence: 99%

Photoaffinity inhibition of dipeptide transport in Escherichia coli

Staros¹,

Knowles²

1978

Biochemistry

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“…Their activity seemed to depend on the action of the intact peptide on the microorganisms (20,24,28,29). The case of the phosphonopeptides, in contrast, resembled more closely the dipeptide bacilysin (15,16) and the tripeptide phosphinothricyl-alanyl-alanine (5), which are both hydrolyzed intracellularly to give active amino acid mimetics.…”

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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“…The vast majority of studies indicate that bacterial peptidases are specific for peptides containing L-amino acids joined in normal alinkages (39,57,(72)(73)(74)(75)(76) and only rarely has the cleavage of peptides with D-amino acids (72,75,(77)(78)(79)(80) or peptides containing unusual linkages or derivatives (47,75,(81)(82)(83)(84) been observed. One wonders whether the frequent occurrence of D-amino acids in peptide antibiotics serves as a protective device against the action of intracellular peptidases (85).…”

Section: T H E Specificity O F Peptidase Actionmentioning

confidence: 99%

“…It has already been noted (66,78,(92)(93)(94)97) that certain peptides are inhibitors of growth, and it is not unlikely that simple peptides that stimulate growth or effect other fundamental changes may be found. The type of growth stimulation envisaged is not that to be observed with a single nutritionally exacting organism but rather that concerned with a more fundamental aspect of the general process of growth and differentiation.…”

Section: B Studies With Lactobacillimentioning

confidence: 99%