scholarly journals Triostin A Derived Cyclopeptide as Architectural Template for the Alignment of Four Recognition Units

ChemistryOpen ◽  
2014 ◽  
Vol 3 (4) ◽  
pp. 152-160 ◽  
Author(s):  
Ursula M. Kotyrba ◽  
Kevin Pröpper ◽  
Eike-F. Sachs ◽  
Anastasiya Myanovska ◽  
Tobias Joppe ◽  
...  
Keyword(s):  
Triostin A

scholarly journals Bifunctional intercalation and sequence specificity in the binding of quinomycin and triostin antibiotics to deoxyribonucleic acid

1978 ◽  
Vol 173 (1) ◽  
pp. 115-128 ◽  
Author(s):  
J S Lee ◽  
M J Waring
Keyword(s):  
Binding Constant ◽  
Binding Constants ◽  
Sequence Specificity ◽  
Peptide Antibiotics ◽  
Naturally Occurring ◽  
Binding Isotherms ◽  
Triostin A ◽  
Specificity Pattern ◽  
Intercalating Agents ◽  
Binding Curves

Quinomycin C, triostin A and triostin C are peptide antibiotics of the quinoxaline family, of which echinomycin (quinomycin A) is also a member. They all remove and reverse the supercoiling of closed circular duplex DNA from bacteriophage PM2 in the fashion characteristic of intercalating drugs, and the unwinding angle at I 0.01 is, in all cases, almost twice that of ethidium. Thus, as with echinomycin, they can be characterized as bifunctional intercalating agents. For the triostins this conclusion has been confirmed by measurements of changes in the viscosity of sonicated rod-like DNA fragments; the helix extension was found to be almost double that expected for a simple monofunctional intercalation process. For triostin A, further evidence for bifunctionality was derived from the cross-over point of binding isotherms to nicked circular and closed circular bacteriophage-PM2DNA. Binding curves for the interaction of quinomycin C and triostin A with a variety of synthetic and naturally occurring nucleic acids were determined by solvent-partition analysis, but triostin C was too insoluble in aqueous solution to make this method applicable. For quinomycin C the highest binding constant was found with Micrococcus lysodeikticus DNA, and its pattern of specificity among natural DNA species was broadly similar to that of echinomycin, although the binding constants were 2–6 times as large. For triostin A the highest binding constant was again found for M. lysodeikticus DNA, but the specificity pattern was quite different from that of the quinomycins. In particular, triostin A bound better to poly(dA-dT) than to the poly(dG-dC) whereas this order was reversed for quinomycin C. There was also evidence that the binding to poly(dA-dT) might be co-operative in nature. No significant interaction could be detected with poly(dA).poly(dT) or with RNA from Escherichia coli. Poly(dG).poly(dC) gave variable results, depending on the source of the polymer. The different patterns of specificity displayed by the quinomycins and triostins are tentatively ascribed to differences in their conformations in solution.

Origin of slow conformer conversion of triostin A and interaction ability with nucleic acid bases

2009 ◽  
Vol 21 (5) ◽  
pp. 541-545 ◽  
Author(s):  
NAOKI HIGUCHI ◽  
YOSHIMASA KYOGOKU ◽  
MASARU SHIN ◽  
KEN INOUYE
Keyword(s):  
Nucleic Acid ◽  
Nucleic Acid Bases ◽  
Triostin A

scholarly journals Synthetic Studies on Quinoxaline Antibiotics. II. Synthesis of Triostin A

1984 ◽  
Vol 57 (8) ◽  
pp. 2203-2210 ◽  
Author(s):  
Masaru Shin ◽  
Ken Inouye ◽  
Hideo Otsuka
Keyword(s):  
Triostin A ◽  
Synthetic Studies

scholarly journals Improved Production of Triostin A in Engineered Escherichia coli with Furnished Quinoxaline Chromophore by Design of Experiments in Small-Scale Culture

2008 ◽  
Vol 24 (1) ◽  
pp. 134-139 ◽  
Author(s):  
A.P. Praseuth ◽  
M.B. Praseuth ◽  
H. Oguri ◽  
H. Oikawa ◽  
K. Watanabe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Design Of Experiments ◽  
Small Scale ◽  
Triostin A ◽  
Engineered Escherichia Coli

Syntheses of Triostin A Antibiotic and Nucleobase-Functionalized Analogs as New DNA Binders

2009 ◽  
Vol 2009 (28) ◽  
pp. 4801-4809 ◽  
Author(s):  
Anmol Kumar Ray ◽  
Ulf Diederichsen
Keyword(s):  
Triostin A ◽  
Dna Binders
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