2006
DOI: 10.2174/157018006775789766
|View full text |Cite
|
Sign up to set email alerts
|

Design, Synthesis, and Antibacterial Activity of Novel Carbacephems

Abstract: Syntheses of (±)-cis-3-hydroxycarbonyl-7-(phenylacetamido)carbacephem (10 ), (±)-cis-3-methoxycarbonyl-7-(phenylacetamido)carbacephem (11 ), (±)-cis-2-chloro-3-hydroxycarbonyl-7-(phenylacetamido)carbacephem (14 ), and (±)-cis-2-chloro-3-methoxycarbonyl-7-(phenylacetamido)carbacephem (15 ) were accomplished. These four heretofore undescribed compounds 10 , 11 , 14 , and 15 showed notable activity against Staphylococcus aureus FDA 209P, Escherichia coli ATCC 39188, Pseudomonas aeruginosa 1101-75, Klebsiella pneu… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
8
0

Year Published

2006
2006
2009
2009

Publication Types

Select...
5

Relationship

0
5

Authors

Journals

citations
Cited by 8 publications
(9 citation statements)
references
References 12 publications
(23 reference statements)
1
8
0
Order By: Relevance
“…Also, the m-value has been used as index of the amount of protein surface exposed to the solvent upon unfolding. A similar dependence on accessible surface area has been demonstrated for heat capacity changes ( C P ) for a set of proteins [38,39]. The m-values and heat capacity changes correlate well with each other, and the C P of a protein is linearly related to the fraction of its hydrophobic residues [40,41].…”
Section: Resultssupporting
confidence: 60%
“…Also, the m-value has been used as index of the amount of protein surface exposed to the solvent upon unfolding. A similar dependence on accessible surface area has been demonstrated for heat capacity changes ( C P ) for a set of proteins [38,39]. The m-values and heat capacity changes correlate well with each other, and the C P of a protein is linearly related to the fraction of its hydrophobic residues [40,41].…”
Section: Resultssupporting
confidence: 60%
“…Furthermore, the red shift of maximum wavelength confirms the folded state of intermediate relative to the native state indicating that a folded structure is formed. However, if the blue shift of Soret band happens, then less folded structure would form [66,67]. The absorption spectra at different concentrations of DTAB show an isosbestic point at 429 nm.…”
Section: Uv-visible Spectramentioning
confidence: 98%
“…5A, column 11). The exceedingly increased ANS fluorescence intensity, as the result of decreased SDS concentration (nanomolar range), demonstrated the more significant exposure of hydrophobic sites of insulin [41,42]. The transfer of ANS from a polar to a non-polar environment led to increased fluorescence intensity and a blue shift (Fig.…”
Section: Ans Fluorescence Studies Of Insulinmentioning
confidence: 94%
“…At this range of SDS concentration, the interactions between insulin and SDS molecules are mainly hydrophobic, although simultaneous repulsive electrostatic interactions between negative charged groups of the protein and negative charged head group of SDS can also occur. However, at low SDS concentrations (0.1-1 M), the interactions are mainly electrostatic repulsion [41,42]. These initial interactions presumably cause insulin to unfold and expose additional hydrophobic sites to the aqueous environment.…”
Section: Ans Fluorescence Studies Of Insulinmentioning
confidence: 99%