• Molecules and Cells
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• 제20권1호
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• pp.1-16
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• 2005

The peptidyl transferase center (PTC) is located in a protein free environment, thus confirming that the ribosome is a ribozyme. This arched void has dimensions suitable for accommodating the 3'ends of the A-and the P-site tRNAs, and is situated within a universal sizable symmetry-related region that connects all ribosomal functional centers involved in amino-acid polymerization. The linkage between the elaborate PTC architecture and the A-site tRNA position revealed that the A-to P-site passage of the tRNA 3'end is performed by a rotatory motion, which leads to stereochemistry suitable for peptide bond formation and for substrate mediated catalysis, thus suggesting that the PTC evolved by genefusion. Adjacent to the PTC is the entrance of the protein exit tunnel, shown to play active roles in sequence-specific gating of nascent chains and in responding to cellular signals. This tunnel also provides a site that may be exploited for local co-translational folding and seems to assist in nascent chain trafficking into the hydrophobic space formed by the first bacterial chaperone, the trigger factor. Many antibiotics target ribosomes. Although the ribosome is highly conserved, subtle sequence and/or conformational variations enable drug selectivity, thus facilitating clinical usage. Comparisons of high-resolution structures of complexes of antibiotics bound to ribosomes from eubacteria resembling pathogens, to an archaeon that shares properties with eukaryotes and to its mutant that allows antibiotics binding, demonstrated the unambiguous difference between mere binding and therapeutical effectiveness. The observed variability in antibiotics inhibitory modes, accompanied by the elucidation of the structural basis to antibiotics mechanism justifies expectations for structural based improved properties of existing compounds as well as for the development of novel drugs.

• 한국응용과학기술학회지
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• 제18권3호
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• pp.180-185
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• 2001

Antibiotics polymer prepared by chemical bonding and simple blending of antibacterial into polymers have attracted much interest because of their long-lasting and antibacterial activity. Antibiotics polymer can significantly reduce losses associated with dissolution, photolytic decomposition and volatillization. Further more, increased efficiency safety and selectivity are additional benefits which may be realized. In this study, Antibiotics polymer was synthesized by chemical reaction of polyacrylic acid with sulfamethazine by N,N'-dicyclohexylcarbodiimide(DCC) method. Antibacterial susceptibility was determined against Streptococcus pyrogenes[gram(+)] and Esherichia coli.[gram(-)] using a standardized disc test. As a result, the synthetic antibiotics polymer exhibited the broad susceptibilty against Streptococcus pyrogenes and Esherichia coli. Especially, the antibiotic effect of antibacterial polymer against Gram negative(Esherichia coli) was much stronger than that against Gram positive(Streptococcus pyrogenes).

• Journal of Electrochemical Science and Technology
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• 제2권3호
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• pp.143-145
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• 2011

Metal-binding antibiotics are very attractive choices as cation selective ionophores. The ability of tetracycline (TC) antibiotics to bind to metal ions has obtained much attention. TCs exhibit the potentiometric performance changes for various cations dependant on several experiment conditions. In this report, we investigated the potentiometric performance changes of TC as the modification of TC's possible metal binding site. We found that the selectivity alter with the blocking main binding site of ionophores for cations. And, additionally it is possible to control the selectivity of sensors with chemical modification of ionophores.

• Bulletin of the Korean Chemical Society
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• 제29권1호
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• pp.165-167
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• 2008

The performances of tetracycline based cation selective polymeric membrane electrodes of many sets with different plasticizers were investigated as the selectivity of ion-selective electrodes and optodes are greatly influenced by membrane solvent and also controlled by plasticizers. The membrane 1 with Bis(2-ethylhexyl) sebacate (DOS) and additive shows good potentiometric performance toward Ca2+ (slope: 27.8 mV per decade; DL: -4.52) including selectivity. Contrastingly, membrane 4 with Dibutyl phthalate (DBP) shows near-Nernstian response, it has also shown the best measuring range and detection limit for Ca2+ (29.5 mV and -5.10) and Mg2+ (24.4 mV and -5.04) and the least selectivity has been also observed between Ca2+ and Mg2+. When the membrane 1 and 4 were used together to flow system, we could determine the concentration of Ca2+ and Mg2+, simultaneously.

• 한국자기공명학회논문지
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• 제21권3호
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• pp.78-84
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• 2017

Pseudin is a naturally occurring 24 amino-acid-residue antimicrobial peptide derived from the skin of paradoxical frog Pseud's paradoxa. It shows potency against the bacteria and antibiotic-resistant bacteria strain, but has high cytotoxicity against mammalian cell. In our previous study, substitution of $Pro^{11}$ for Gly (Ps-P) increased bacterial cell selectivity but decreased the antibacterial activity of pseudin. In this study, we designed pseudin analogue, Ps-4K-P with increased cationicity up to +7 in Ps-P by substituting Glu14, Gln10, Gln24, and Leu18 with Lys. Ps-4K-P showed improved potent antibacterial activity with high bacterial cell selectivity. We determined the tertiary structure of Ps-4K-P in the presence of DPC micelles by NMR spectroscopy and it has a hinge structure at $Pro^{11}$ followed by three turn helices from $Pro^{11}$ to $Val^{23}$ at the C-terminus. Amphipathicity with increased cationicity as well as helix-hinge-helix structural motif provided by introduction of a Pro at position $Gly^{11}$ are the crucial factors which confer antibacterial activity with bacterial cell selectivity to Ps-4K-P.

• Journal of Dairy Science and Biotechnology
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• 제42권1호
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• pp.9-17
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• 2024

This study aimed to evaluate the appropriateness of MRS-C (0.05% L-cystein; pH 5) and BHI-CM (0.05% L-cystein, 0.5% mucin) agars for the selective isolation of bifidobacteria in fecal samples compared to blood-liver-NPNL (BL-NPNL) agar. Over 200 isolated colonies were characterized morphologically and biochemically. Genomic DNA was extracted from pure cultures of the isolated strains, followed by PCR amplification of the 16S rRNA gene. Bifidobacterium longum and B. animalis were selectively isolated from MRS-C agar and Lactobacillus acidophilus and Enterococcus avium were also isolated. B. longum, B. faecale, and B. animalis were isolated from feces on BHI-CM agar; however, different Bacteroides strains (including Bac. fragilis, Bac. kiribbi, Bac. ovatus, Bac. koreensis, and Bac. salyersiae) were also detected. BL-NPNL agar successfully isolated B. longum and Bacillus, while other Bifidobacterium and Bacteroides species could not grow owing to the presence of antibiotics in the medium. The use of antibiotics in a medium can enhance the selectivity; however, antibiotics may inhibit the growth of certain bacteria in a sample. Hence, adjusting pH or adding non-antibiotic nutrients to the medium is more advantageous, than relying on antibiotics.

• 한국식품위생안전성학회지
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• 제5권3호
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• pp.159-164
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• 1990

To detect and quantitation residual antibiotics and antibacterial agents in meats, we performed a biological assay employing the three microorganisms Bacillus subtilis ATCC 6633, Micrococcus luteus ATCC 9341, and Bacillus cereus var. mycoides ATCC 11778 for the screening purpose and developed a Gas Chromatography-mass Spectrometry(GC/MS) analysis for the confirmation and quantiation. In the biological assay (paper disk method), three test solution are used depending on the character of the residual antibiotics and antibacterial agents, follow by a simple clean up procedure which includes homogenization with Mcilvaine buffer, defatting with includes homogenization with Mcilvaine buffer, defatting with hexane, extraction with chloroform, clean-up by Sep-Pak $C_{18}$ and Bakerbond SPE carboxylic acid column. The chloroform layer is used for the analysis of sulfa agents. macrolides antibiotics and antibacterial agents, Adsorbed materials in the Sep-Pak $C_{18}$ were also employed for th analysis of penicillins and tetracyclines. Effluents from the Sep-Pak $C_{18}$ were cleaned-up one more by Bakerbond 10 SPE COOH column and employed for the analysis of aminoglycosides. In the instrumental analysis by using the GC/MSD, residual antibiotics and antibacterial agent were quantitated by selected ion monitoring (SIM) mode after derivatization. A simultaneous analysis of six residual antibiotic and antibacterial agent such as oxytetracycline, penicillin, ampicillin, choliraphenicol and thiamphenicol was developed with simple cleanup procedures revealing good recovery and reproducibility. Also, simultaneous detection of macrolides antibiotics such as erythromycin, spiramycin, and oleandomycin was developed after acid hydrolysis due to their large molecular structures. Because of the high reproducibility and selectivity of these two methods, it is very desirable that the combination of the two methods be used in the bioassay for the screening of residual antibiotics and antibacterial agent and that GC/MSD analysis be used for the confirmation and quantitation.

• 한국응용과학기술학회지
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• 제17권3호
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• pp.198-202
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• 2000

PVA blend films were prepared by solution blending method for the purpose of useful antibiotic polymers. Characteristics properties of blending films such as elongation and tensile strength were determined. Tensile strength and elongation were rapidly reduced as increasing the blending ratio of natural polymer. Blend films were found that phase separation was occured as more than 25wt% increasing the blend ratio of chitosan. Also, The antibiotics of blend films were examined against gram(+) and gram(-) by disk susceptibility test. As a result, kind of blending films to show the highest antibiotics was chitosan 20wt% and the selectivity of mold strain was observed.

• Bulletin of the Korean Chemical Society
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• 제33권9호
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• pp.2883-2889
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• 2012

LL-37 is the only antimicrobial peptide (AMP) of the human cathelicidin family. In addition to potent antimicrobial activity, LL-37 is known to have the potential to inhibit lipolysaccharide (LPS)-induced endotoxic effects. To provide the stability to proteolytic digestion and increase prokaryotic selectivity and/or anti-endotoxic activity of two Lys/Trp-substituted 19-meric antimicrobial peptides (a4-W1 and a4-W2) designed from IG-19 (residues 13-31 of LL-37), we synthesized the diastereomeric peptides (a4-W1-D and a4-W2-D) with D-amino acid substitution at positions 3, 7, 10, 13 and 17 of a4-W1 and a4-W2, respectively and the enantiomeric peptides (a4-W1-E and a4-W2-E) composed D-amino acids. The diastereomeric peptides exhibited the best prokaryotic selectivity and effective protease stability, but no or less anti-endotoxic activity. In contrast, the enantiomeric peptides had not only prokaryotic selectivity and anti-endotoxic activity but also protease stability. Our results suggest that the hydrophobicity and ${\alpha}$-helicity of the peptide is important for anti-endotoxic activity. In particular, the enantiomeric peptides showed potent anti-endotoxic and LPS-neutralizing activities comparable to that of LL-37. Taken together, both a4-W1-E and a4-W2-E holds promise as a template for the development of peptide antibiotics for the treatment of endotoxic shock and sepsis.

• Journal of Microbiology and Biotechnology
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• 제28권5호
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• pp.671-678
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• 2018

Papiliocin, isolated from the swallowtail butterfly (Papilio xuthus), is an antimicrobial peptide with high selectivity against gram-negative bacteria. We previously showed that the N-terminal helix of papiliocin (PapN) plays a key role in the antibacterial and anti-inflammatory activity of papiliocin. In this study, we measured the selectivity of PapN against multidrug-resistant gram-negative bacteria, as well as its anti-inflammatory activity. Interactions between Trp2 of PapN and lipopolysaccharide (LPS), which is a major component of the outer membrane of gram-negative bacteria, were studied using the Trp fluorescence blue shift and quenching in LPS micelles. Furthermore, using circular dichroism, we investigated the interactions between PapN and LPS, showing that LPS plays critical roles in peptide folding. Our results demonstrated that Trp2 in PapN was buried deep in the negatively charged LPS, and Trp2 induced the ${\alpha}$-helical structure of PapN. Importantly, docking studies determined that predominant electrostatic interactions of positively charged arginine residues in PapN with phosphate head groups of LPS were key factors for binding. Similarly, hydrophobic interactions by aromatic residues of PapN with fatty acid chains in LPS were also significant for binding. These results may facilitate the development of peptide antibiotics with anti-inflammatory activity.