New Perspectives in the Chemistry and Biochemistry of the Tunichromes and Related Compounds

Taylor, Steven W.; Kammerer, Bernd; Bayer, Ernst

doi:10.1021/cr940467q

Cited by 119 publications

(107 citation statements)

References 94 publications

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“…Vanadium occurs as an "essential trace" element in diverse living forms [1][2][3][4][5][6]. It plays active roles in many enzymatic reactions such as halogenation of organic substrate [2,5,6] and fixation of nitrogen through an alternative pathway [2,[7][8][9].…”

Section: Dna Cleavage Binding and Intercalation Studies Of Drug-basementioning

confidence: 99%

DNA cleavage, binding and intercalation studies of drug-based oxovanadium(IV) complexes

Patel

Chhasatia

Patel

et al. 2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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The complexes of oxovanadium(IV) with ciprofloxacin and various uni-negative bidentate ligands have been prepared and their structure investigated using spectral, physicochemical and elemental analyses. The viscosity measurement suggest that the complexes bind to DNA by intercalation. The DNA binding efficacy was determined using absorption titration to obtain the binding constant (K b ). The DNA cleavage efficacy was determined using gel electrophoresis. The DNA binding and cleavage efficacy were increased in the complexes relative to the parental ligands and metal salts. Antibacterial activity has been assayed against two Gram (2 ve) i.e. Escherichia coli, Pseudomonas aeruginosa and three Gram ( þ ve) Staphylococcus aureus, Bacillus subtilis, Serratia marcescens microorganisms using the doubling dilution technique. The results show a significant increase in antibacterial activity in the complexes compared with parental ligands and metal salts.

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Section: Dna Cleavage Binding and Intercalation Studies Of Drug-basementioning

confidence: 99%

DNA cleavage, binding and intercalation studies of drug-based oxovanadium(IV) complexes

Patel

Chhasatia

Patel

et al. 2009

Journal of Enzyme Inhibition and Medicinal Chemistry

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“…Typically, one expects such peptides to be cationic and amphipathic molecules with 16 to 40 residues (87), although two bovine peptides, dodecapeptide and indolicidin, are 12 to 13 amino acids long. In addition, plicatamide and other ascidian peptides (4,(85)(86)(87), including the halocyamines (below), are characterized by an oxidatively decarboxylated aromatic C-terminal residue. This structural feature may represent an alternative to C-terminal amidation for conferring proteolytic resistance and removal of the carboxylate's negative charge.…”

Section: Chordatamentioning

confidence: 99%

Antimicrobial Peptides from Marine Invertebrates

Tincu

Taylor

2004

Antimicrob Agents Chemother

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299

135

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“…Emulation has been largely limited to adapting Dopa (3,4-dihydroxyphenyl-L-alanine), a catecholic amino acid in mussel adhesive proteins, for a variety of synthetic polymers. Dopa also occurs in the cement of sandcastle worms and tunicates, among others (Taylor et al, 1997;Waite et al, 1992). The reluctance of biotechnology to mimic anything but Dopa is unfortunate, because mussels offer profound insights at multiple length scales and time scales for implementing wet adhesion; even the successful translation of Dopa for adhesion technology depends on a deeper understanding of how mussels regulate the chemistry of catechols (see Glossary).…”

Section: Introductionmentioning

confidence: 99%

Mussel adhesion – essential footwork

Waite

2017

Journal of Experimental Biology

528

744

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Robust adhesion to wet, salt-encrusted, corroded and slimy surfaces has been an essential adaptation in the life histories of sessile marine organisms for hundreds of millions of years, but it remains a major impasse for technology. Mussel adhesion has served as one of many model systems providing a fundamental understanding of what is required for attachment to wet surfaces. Most polymer engineers have focused on the use of 3,4-dihydroxyphenyl-L-alanine (Dopa), a peculiar but abundant catecholic amino acid in mussel adhesive proteins. The premise of this Review is that although Dopa does have the potential for diverse cohesive and adhesive interactions, these will be difficult to achieve in synthetic homologs without a deeper knowledge of mussel biology; that is, how, at different length and time scales, mussels regulate the reactivity of their adhesive proteins. To deposit adhesive proteins onto target surfaces, the mussel foot creates an insulated reaction chamber with extreme reaction conditions such as low pH, low ionic strength and high reducing poise. These conditions enable adhesive proteins to undergo controlled fluid-fluid phase separation, surface adsorption and spreading, microstructure formation and, finally, solidification.

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New Perspectives in the Chemistry and Biochemistry of the Tunichromes and Related Compounds

Cited by 119 publications

References 94 publications

DNA cleavage, binding and intercalation studies of drug-based oxovanadium(IV) complexes

DNA cleavage, binding and intercalation studies of drug-based oxovanadium(IV) complexes

Antimicrobial Peptides from Marine Invertebrates

Mussel adhesion – essential footwork

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