Poly‐p‐methylstyrene obtained with n‐amylsodium

Higashi, Hiromi; Tanaka, Takehide; Tanimura, Masamitsu; Egashira, Takashi

doi:10.1002/macp.1961.020430126

Cited by 7 publications

(5 citation statements)

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“…This inhibition thus serves as the key step in the inhibition of cell wall synthesis by this antibiotic. 63 Recent solid-state total synthesis of the enantiomer of Bc showed a similar activity as Bc in vitro, suggesting non-stereo-specific interaction for the antibiotic activity of this antibiotic which was suggested to be the achiral long-chain bactoprenyl-pyrophosphate. 64 Although a pyrophosphate-metal-bacitracin ternary complex was proposed 65 detailed binding and structural information about this ternary complex was lacking.…”

Section: Antibiotic Peptidyl Bacitracinmentioning

confidence: 95%

Metallopeptides — from Drug Discovery to Catalysis

Ming

2010

J Chinese Chemical Soc

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Oligopeptides are involved in diverse biological activities, including neurotransmission and antibiotic. Many natural-occurring peptides and peptide-ketide hybrids exhibit specific biological activities and chemical reactivities upon binding with certain metal ions, such as divalent metal-binding antibiotic bacitracin and anticancer Fe/Cu-bleomycin. There are also numerous synthetic peptides designed to bind metal ions to exhibit wide range of physical properties and chemical and biological activities. In this review we summarize the background and discuss our research on metal binding properties, structures, and chemical reactivities of three metallopeptides, the bacterial antibiotic bacitracin, the Alzheimer's disease-related b-amyloid, and the salivary antimicrobial histatin. Despite their different structures and biological functions, the Cu 2+ complexes of these peptides exhibit significant activities toward catechol oxidation and phenol hydroxylation. However, the mechanisms of the oxidative reactions among these three Cu-peptides seem to be distinctively different. Our current understanding about the structure-bioactivity relationship and chemical reactivities as well as implications in drug discovery of these peptides are summarized herein.

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Section: Antibiotic Peptidyl Bacitracinmentioning

confidence: 95%

Metallopeptides — from Drug Discovery to Catalysis

Ming

2010

J Chinese Chemical Soc

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“…Many membrane proteins are difficult to solubilize under these conditions [7] , others tend to aggregate irreversibly [67], and still others are unstable in aqueous solutions [76]. Furthermore, these difficul-280 ties may occur even in the presence of detergents and other denaturing reagents [67] .…”

Section: Solubilization Of Membrane Proteinsmentioning

confidence: 99%

“…The recent work of Strominger's group has indicated the possibility of extracting membrane proteins directly into organic solvents without denaturation [76] . In principle this is a very sensible way of handling such proteins, although it may not always be successful [7].…”

Section: Solubilization Of Membrane Proteinsmentioning

confidence: 99%

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Isolation and study of functional membrane proteins Present status and future prospects

Chavin

1971

FEBS Letters

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“…This compound functions as a carrier molecule in the biosynthesis of the peptidoglycan and other polysaccharides of bacterial cell walls [l]. The phosphokinase is insoluble in water but is soluble in butanol and other organic solvents [2].…”

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confidence: 99%

The Reactivation of C₅₅‐Isoprenoid‐Alcohol‐Phosphokinase Apoprotein by Lipids

Sandermann

1974

European Journal of Biochemistry

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1.The reactivation of C,,-isoprenoid-alcohol phosphokinase apoprotein by a variety of lipids has been investigated.2. A considerable lack of specificity for the chemical structure of the activating lipid is demonstrated.3. Reactivation appears to occur by some physical mechanism. A n electrostatic interaction of protein and lipid does not appear to be important.4. All active lipids found are able to swell and become hydrated in aqueous buffer. Some of these lipids were active only after sonication or in the presence of detergent.5. The hydrated lipid phase is concluded to activate by solubilization, as a liquid-crystalline or micellar solvent for the extremely hydrophobic enzyme apoprotein and for the non-hydrating C,,-isoprenoid alcohol.The enzyme C,,-isoprenoid-alcohol phosphokinase from the membrane of Staphylococcus aureus catalyzes the ATP-dependent formation of C5,-isoprenyl monophosphate. This compound functions as a carrier molecule in the biosynthesis of the peptidoglycan and other polysaccharides of bacterial cell walls [l]. The phosphokinase is insoluble in water but is soluble in butanol and other organic solvents [2].Using organic solvents throughout the purification procedure the enzyme has been purified essentially to homogeneity by newly developed techniques [3,4]. The enzyme apoprotein consists of a single polypeptide chain of molecular weight 17 000 [3,5]. It might be the most hydrophobic protein described so far as judged from its amino-acid composition and from its partition coefficient in butanol-water [5]. The enzyme requires the presence of a lipid "cofactor" for activity [6]. A previous analysis of Arrhenius plots for the reactivation of enzyme apoprotein by synthetic lecithins suggested that the enzyme reaction might occur at the aqueous interface of mixed micelles consisting of the lecithin cofactor, the C,,-isoprenoid-alcohol substrate and the enzyme apoprotein I n this investigation the specificity and some other parameters involved in the activation of the enzyme apoprotein (and of the C,,-isoprenoid alcohol) by lipids have been studied. It is suggested that the extremely hydrophobic enzyme apoprotein and the water-insoluble C,,-isoprenoid alcohol are activated by the well-known phenomenon of solubilization in a hydrated lipid phase. The enzyme reaction is thought to occur a t the aqueous interface of the resulting lipoprotein complex. Some of the results have been reported in preliminary communications [S, 91. MATERIALS AND METHODSC,,-isoprenoid-alcohol phosphokinase apo-protein wa8 purified about 1000-fold from the membrane of Staphylococcus aureus, strain H, through step 6 of the procedure described earlier [3,4]. The preparation employed contained 2Opg protein per ml of a solution of 0.6 M ammonium acetate in methanoln-butanol 1 : 1. [y-3aP]ATP was purchased from New England Nuclear, Boston. Ficaprenol was prepared from leaves of Picus elastica [lo]. The lipids employed %,were obtained from the sources indicated in Table 1. Span detergents were obtained

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Poly‐p‐methylstyrene obtained with n‐amylsodium

Cited by 7 publications

References 3 publications

Metallopeptides — from Drug Discovery to Catalysis

Metallopeptides — from Drug Discovery to Catalysis

Isolation and study of functional membrane proteins Present status and future prospects

The Reactivation of C₅₅‐Isoprenoid‐Alcohol‐Phosphokinase Apoprotein by Lipids

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Poly‐p‐methylstyrene obtained with n‐amylsodium

Cited by 7 publications

References 3 publications

Metallopeptides — from Drug Discovery to Catalysis

Metallopeptides — from Drug Discovery to Catalysis

Isolation and study of functional membrane proteins Present status and future prospects

The Reactivation of C55‐Isoprenoid‐Alcohol‐Phosphokinase Apoprotein by Lipids

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The Reactivation of C₅₅‐Isoprenoid‐Alcohol‐Phosphokinase Apoprotein by Lipids