Technology should therefore be used to link the three partners (p

Technology should therefore be used to link the three partners (patient, pharmacist, GP), with each having different responsibilities. In such an approach the patient will be responsible for managing their medicines according to an agreed schedule, carrying

out the home monitoring and providing feedback on symptom control through the connected health equipment. The results of this engagement will then be relayed (wirelessly or via landline linkage) to a central (web-based) data platform, which will automatically send back a positive, supportive message to the patient if control is being achieved. When disease management markers become out of control, they will automatically trigger an alert message to be sent to the patient and also to the GP or pharmacist (or both) for appropriate action to be taken. Having reviewed see more the findings, the GP or pharmacist

could then send a text message to the home base unit or telephone the patient to give advice. This type of approach could also be delivered from a hospital base (hospital doctor and clinical pharmacist), for example, during the first month (highest risk period for readmission) after a patient has been hospitalised, before ‘discharging’ the patient to the primary care providers when the patient is deemed to be stabilised. This ‘ward in the community’ concept could be a useful approach to addressing high readmission rates. Continued support could be provided from the hospital pharmacy team if community pharmacists do not wish to become engaged. There are some examples of pharmacist ABT199 engagement in

‘connected health’ in published studies to date, however, these have been the exception. Although a recent study in the New England Journal of Medicine (evaluating a telemonitoring programme for heart failure patients) provided no evidence of benefit, further research is urgently required within this ‘space’ as isothipendyl monitoring equipment becomes more sophisticated and user friendly. It is clear that not all patients will have the required self-efficacy to fully participate in this type of programme, or may have issues around privacy, and a test of suitability may need to be developed, in much the same way as a genomics test is used in personalised medicine. This would allow alternate approaches to care provision to be considered and help prevent unnecessary spend on equipment that will remain unused. It is clear that further rapid developments will be made in the connected health world in the near future. Pharmacists must become engaged or find themselves further excluded from the care of patients with chronic illness and pharmacy practice researchers must assist by providing the evidence base for this new paradigm in chronic disease management.

g the hexapeptide hydrazide 3, Fig 1) The results obtained in

g. the hexapeptide hydrazide 3, Fig. 1). The results obtained in assays with vanOxyB and balOxyB are summarized in Table 2. Intriguingly, all of the electron transfer proteins are able to effectively donate two electrons to vanOxyB during the catalytic cycle, using the hexapeptide–PCP

APO866 cost (1) as a substrate, with conversions to monocyclic product (3), under the standard conditions, ranging from 60 to over 90%. The heptapeptide–PCP (2, Fig. 1), however, is less efficiently converted into the corresponding monocyclic product, with conversions from 10% to 60% observed. It is important, however, to note that this heptapeptide substrate (2) is a mixture of inseparable diastereomers GSI-IX cell line (which arise during the synthesis of the substrate) differing in configuration at C(α) in residue-7. The results also suggest a more favorable interaction between vanOxyB

and spinFd or balFd-VII, than between vanOxyB and ecoFld or balFd-V. Similar findings were obtained in activity assays using balOxyB. In this case, however, the differences in substrate turnover achieved with the four electron transfer proteins, and between the hexa- and heptapeptide substrates, are more pronounced. Assays with balOxyB and ecoFld or balFd-V showed only a marginal turnover of hexapeptide (1) to a monocyclic product (3). However, with spinFd and especially with balFd-VII, significant cyclization of the substrate was observed (Table 2), with conversion of most hexapeptide to monocycle similar to that seen in assays with vanOxyB. However, the turnover of heptapeptide (2) was significantly lower, with the best result

being 15% conversion to a monocyclic product achieved with balFd-VII. These results suggest a higher discrimination between the hexa- and heptapeptides, with the hexapeptide being more strongly favored as a substrate by balOxyB. Finally, these findings also indicate degeneracy in the ability of various different Fds to support the catalytic activities of P450 coupling enzymes from different glycopeptide-producing organisms. This property may well make it difficult to assign a specific function to each of the individual Fds identified in the A. balhimycina genome, at least using in vitro assays. On the other hand, this flexibility should be an advantage in facilitating more detailed in vitro studies of these interesting cytochrome P450 cross-linking enzymes. The authors thank the Swiss National Science Foundation and the EU 6th framework program for supporting the project COMBIGTOP (LSHB-CT-2003-503491). “
“The existence of large number of a member of the Bacteroidetes in NaCl-saturated brines in saltern crystallizer ponds was first documented in 1999 based on fluorescence in situ hybridization studies. Isolation of the organism and its description as Salinibacter ruber followed soon.

Sortases catalyze the assembly of surface proteins and fimbriae i

Sortases catalyze the assembly of surface proteins and fimbriae in the cell wall envelope of gram-positive bacteria. SrtC1 is required for the biosynthesis of type 1 fimbriae in A. oris T14V (Chen et al., 2007). In order to better understand the structure–function of this sortase, we analyzed the role of eight conserved amino acid residues. The amino acids to be mutated were chosen based on the sequence alignment

of several class C family sortases (Fig. 2). Each mutation was first introduced in vitro into plasmid p6Srt carrying the srtC1 gene (Chen et al., 2007) by site-directed mutagenesis to replace each conserved amino acid with an alanine residue. The desired mutations were confirmed by sequencing and the integrity of all plasmid constructs was verified by enzyme digestions and sequencing. The mutated srtC1 copies were introduced into the srtC1 deletion host strain ΔSrtC1 (Chen et al., 2007) by transformation. Epigenetics Compound Library supplier STA-9090 in vivo The resultant transformants were confirmed for the presence of mutated srtC1 introduced by allelic exchange. Cell surface proteins from these mutants were extracted, separated on gel and probed with monoclonal antibody against the type 1 structural subunit FimP. The ability to assemble type

1 fimbriae, as indicated by the polymerization of FimP, was used to evaluate the activity of mutated sortases. As shown by the results of the Western blot (Fig. 3), five mutants (H184A, L263A, T265A, F213A and R275A) produced patterns of surface proteins similar to those of the wild type, displaying the polymeric form of the structural subunits in the high-molecular-weight region as revealed by the anti-FimP antibody. However, only the monomeric form

of FimP was observed in the other three mutants, H204A, Y236A and C266A. The results indicate that each of these three mutations either abolished the SrtC1 activity, or reduced the activity to an undetectable level as revealed by the blot method, or that these three mutated sortases might not be expressed and/or stable compared with the wild-type SrtC1. Dot-blot results indicate that there are less FimP components on the surfaces of these three mutants than on those of the wild-type strain and other mutants (Fig. S1). There is a conserved TLXTC motif in all indentified sortases. The Cys residue in this motif is essential for during any sortase activity. Based on the newly published crystal structure of SrtC1(Persson, 2011), the nucleophile Cys 266 is located at the centre of the active site. The effect of C266A mutation is consistent with the hypothesis that this catalytic cysteine residue is used in the nucleophilic attack of the Thr-Gly peptidic bond in the target’s LPXTG motif. A similar mutation effect has also been reported for both nonpilus-related and pilus-related sortases from other organisms. For example, Cys 184 in SrtA from Staphylococcus aureus (Ton-That et al., 1999, 2002; Frankel et al., 2007), Cys 193 in SrtC1 from Streptococcus pneumoniae (Manzano et al.

The Conover test indicated that there was no significant differen

The Conover test indicated that there was no significant difference between those two sub-groups of patients (P = 1.00). Correlation analyses did not show

any signification association between the amount of SI and the PMv–M1 interactions, suggesting an independence of the two phenomena (Table 4). Our results showed that the PMv exerted a modulatory influence on the M1 at rest and during movement preparation, and that this influence was absent in patients. We confirmed that the PMv inhibited the M1 at rest Proteasome inhibitor in controls and that this inhibition was muscle specific. Moreover, contrary to our hypothesis, we showed that this inhibition was not enhanced during movement initiation, indicating that the ipsilateral ventral premotor–motor inhibition does not play a key role in SI in normal subjects. In accordance with the literature, we showed that healthy volunteers presented with SI (regarding the APB muscle) before and at movement onset and that this SI was absent in patients (Sohn & Hallett, 2004a,b; Beck et al., 2008, 2009a,b,c). In parallel with this inhibition, the excitability of the synergist muscle cortical representation was increased before and at movement onset in controls

as well as in patients with FHD without significant differences between the two groups, as previously reported (Beck et al., 2008). Indeed, we showed that MEPFDI was significantly enhanced at T50 and Tpeak. This preserved central excitation, in line with the literature, shows that the cortico-spinal excitability of the synergist muscle is not impaired in patients with FHD. Together with this finding, we did not observe any differences in RTs between patients and controls (Stinear & Byblow, 2005; Beck et al., 2008, 2009a,b). Although RTs as well as the central excitation were not impaired in patients, it is noteworthy that some EEG studies have demonstrated an abnormal motor preparation in patients with FHD. Abnormally reduced Farnesyltransferase event-related

desynchronization or Bereitschaftspotential has been reported in patients with FHD, preceding voluntary, self-paced movements (Deuschl et al., 1995; Ikeda et al., 1996; Yazawa et al., 1999; Toro et al., 2000). Event-related desynchronization and Bereitschaftspotential reflect the activation of premotor and motor areas involved in movement preparation and execution. Abnormal event-related desynchronization or Bereitschaftspotential suggests an impairment of premotor and/or motor cortex activation during self-paced movement preparation. These complementary EEG–TMS data suggest that, although the excitability of the synergist muscle representation over the M1 is preserved in patients with FHD, the premotor–motor interactions preceding voluntary movement are impaired. Our results showed a lack of RT, RMT and rest MEP differences between patients and controls.

7) The OT analysis confirmed these results The proportion of pa

7). The OT analysis confirmed these results. The proportion of patients exhibiting a virological response in an OT analysis was similar over time (Fig. 4). The proportion of patients who developed grade 3–4 adverse events during 48 weeks of treatment was not statistically significantly different between the arms (SQV/r arm, six

of 57 patients; 11%; ATV/r arm, 12 of 61 patients; 20%; P=0.2). Only three of these grade 3–4 adverse events were judged by investigators to be study drug related: hyperbilirubinaemia in two patients and skin rash in another patient. None of the 16 serious adverse events (SQV/r arm, n=8; ATV/r arm, n=8) was judged to be study drug Sirolimus chemical structure related. One patient in the SQV/r arm died during the trial, the death being categorized as sudden death; an autopsy was not performed. Mild-to-moderate loose stools and diarrhoea occurred more frequently in the SQV/r arm (SQV/r arm, n=30; ATV/r arm, n=8), but grade 3–4 gastrointestinal complaints were not reported. Unconjugated hyperbilirubinaemia (grade 2–4) occurred significantly more frequently in the ATV/r arm (SQV/r arm, n=3; ATV/r arm, n=31). We demonstrated noninferiority of the SQV/r-based regimen with respect to changes in TC. Once-daily SQV/r 2000/100 mg and ATV/r 300/100 mg, when

combined with TDF/FTC as initial therapy for HIV-1 infection, had comparable modest effects on TC. In addition, neither of the regimens resulted in significant increases in LDL cholesterol, apoB or TG. This may suggest that both study regimens exert little additional influence on patients’ cardiovascular risk. Findings of observational studies suggest that, although PIs as a class are associated with an increased risk of MI, this is not the case for SQV [30,31]. Data concerning ATV are Orotic acid more sparse, but one case–control study reported that neither SQV nor ATV was significantly associated

with an increased risk of myocardial infarction [32]. Of note, one patient on SQV/r died of sudden death. This may be relevant in light of the recent FDA warning that SQV in healthy volunteers was associated with electrocardiographic QT and PR interval prolongation [33]. Unfortunately, no electrocardiograms were performed in this trial and further details concerning the circumstances of death were not available in our patient. Although there was a numerically greater reduction in insulin sensitivity assessed by HOMA in the ATV/r arm than in the SQV/r arm, this did not reach statistical significance, possibly because of our limited sample size. Of note, a previous hyperinsulinaemic euglycaemic clamp study showed no significant changes in glucose disposal rate after 4 weeks for either treatment [19]. Neither of the regimens was associated with limb fat atrophy or loss of SAT.

g malate and glyoxylate), because a variety of acetate assimilat

g. malate and glyoxylate), because a variety of acetate assimilation pathways convert acetate into Selleck Palbociclib these compounds (e.g. the glyoxylate shunt of the tricarboxylic acid cycle, the ethylmalonyl-CoA pathway, the citramalate cycle, and the methylaspartate cycle). In this review, we summarize the history of facultative methanotrophy, describe scenarios for the basis

of facultative methanotrophy, and pose several topics for future research in this area. Aerobic methanotrophs are widely distributed in the environment, found wherever methane : air interfaces develop, including in wetlands, bogs, agricultural, forest and urban soils, rice paddies, groundwater, landfill cover soils, among many other locations (Semrau et al., 2010). These cells play a critical role in the global carbon cycle by utilizing methane as a source of carbon and energy – it is estimated that in soils, aerobic methanotrophs consume ∼30 Tg methane year−1 (Kolb, 2009). It was initially widely believed

that aerobic methanotrophs were obligate, i.e., that these microorganisms could only grow utilizing methane or methanol, and in some cases, other C1 compounds such as formaldehyde, formate, and methylamine, but not compounds with carbon–carbon bonds (Bowman, 2006). The cause for obligate methanotrophy is still unresolved (Wood et al., 2004), and, interestingly, many reports have recently been published of methanotrophs that also able

to utilize LGK-974 cell line multicarbon PtdIns(3,4)P2 compounds as sole growth substrates (Semrau et al., 2010). Hence, it appears that facultative methanotrophy may be more common than originally thought. In this review, the history and basis of facultative methanotrophy is summarized, as well as the implications and applications of such metabolism. The defining characteristic of a methanotroph is its ability to utilize methane as its sole carbon and energy source, and there are at least two forms of the key enzyme involved in the initial oxidation of methane to methanol, the methane monooxygenase (MMO). Most but not all methanotrophs express a membrane-bound or particulate methane monooxygenase (pMMO), while some can either express in addition, or as the unique form, a cytoplasmic, or soluble methane monooxygenase (sMMO). Phylogenetically, aerobic methanotrophs belong primarily to the Alpha- and Gammaproteobacteria, although recently aerobic methanotrophs have also been found that belong to the Verrucomicrobia phylum (Op den Camp et al., 2009; Semrau et al., 2010). The alphaproteobacterial methanotrophs can be further divided in the Beijerinckiaceae and Methylocystaceae families, while the gammaproteobacterial methanotrophs belong to the Methylococcaceae family.

A pharmacokinetic study in healthy volunteers was reminiscent of

A pharmacokinetic study in healthy volunteers was reminiscent of the saquinavir study, and was terminated early because of high rates of severe transaminitis [101]. Recent data suggest that atazanavir with or without ritonavir boosting had unfavourable pharmacokinetics when administered with rifampicin [102–104]. Trough atazanavir Tyrosine Kinase Inhibitor Library concentration concentrations were reduced by >80% [103]. Tipranavir concentrations were reduced by 80% by rifampicin [105]. The interaction between darunavir and rifampicin has not yet been investigated. In line with other PIs, it is currently recommended that darunavir should not be coadministered with rifampicin. The use of

rifabutin in treating TB in HIV-positive patients is discussed above (see ‘Use of rifapentine’ [EII]). Rifabutin can be administered with unboosted PIs except saquinavir [106], although they will rarely be used in practice. The balance between rifabutin induction and PI inhibition of CYP3A4 means that the dose of rifabutin should be decreased from 300 to 150 mg daily to avoid toxicity [48,70]. If PIs are used with low-dose ritonavir boosting then the dose of rifabutin should be reduced to 150 mg three times per week [49,105]. This recommendation

is derived from pharmacokinetic studies and modelling. There are no clinical outcome data for either HIV or TB using this strategy. Adherence should be monitored closely as the dose of rifabutin would become inadequate if the boosted PI is not taken concomitantly. Where available, drug levels of the PI should be measured. There have been reports of acquired rifabutin resistance occurring even in patients taking rifabutin 150 mg three

times a week with boosted PIs. No rifabutin drug levels were available in those patients and, although there may have been other reasons for these failures, physicians may consider measuring the levels of rifabutin and its active metabolite 25-0-desacetyl rifabutin if results are available in a timely manner [107]. Complex Megestrol Acetate interactions may occur when a rifamycin is given with salvage regimens such as an integrase, boosted PI and an NNRTI. Rifabutin is safer than rifampicin, but there are few data to guide the clinician regarding dose modification. TDM is recommended. We recommend that PI/ritonavir combinations should not be given with rifampicin. [EII] If possible, the HAART regimen should be changed to avoid PIs. If effective HAART necessitates the use of PIs then rifabutin should be used instead of rifampicin. [AII] Raltegravir is metabolized by UGT1A1 glucuronidation. Rifampicin is an inducer of UGT1A1, and reduces trough levels of raltegravir by approximately 60% [108]. Because the antiviral activity of raltegravir 200 mg twice daily was very similar to that of the licensed dose (400 mg twice daily), an earlier recommendation was that standard doses of raltegravir should be used with rifampicin. There is at least one report of raltegravir failure when given like this with rifampicin (S.

Thus, the 753 orthologous gene groups were used as a unique ortho

Thus, the 753 orthologous gene groups were used as a unique orthologous gene dataset to investigate the genetic relationship at the whole-genome level among AAB. Amino acid sequences of the unique orthologous dataset were concatenated into a pseudo-single-sequence and an NJ phylogenetic

tree was constructed from multiple amino acid alignments of the concatenated sequences CP-868596 price (Fig. 3a). The phylogenetic tree showed that Gluconobacter was the first to diverge from its common ancestor with Acetobacter and Gluconacetobacter. This result is in agreement with that of the phylogenetic analysis of 293 metabolic proteins. In addition, two branches of the concatenated proteins showed high statistical confidence (NJ bootstrap value; 100%), suggesting that the phylogeny

of the protein-coding regions of AAB is different from that of the 16S rRNA gene. In addition, some classic markers, Selleckchem PD0325901 DNA gyrase subunit B (GyrB), DNA gyrase subunit A (GyrA), and DNA-directed RNA polymerase subunit β (RpoB), also showed the same phylogenetic pattern as the concatenated phylogenetic tree (data not shown). These genes might be useful to determine phylogenetic relationships, instead of concatenated proteins, in species for which complete genome sequences are not available. It has been reported that A. aceti strain 1023 lacks malate dehydrogenase (Mdh) and succinyl-CoA synthetase (SCS) genes, but can assimilate acetate by a modified TCA cycle, in which Mdh and SCS are functionally replaced by malate : quinone oxidoreductase (Mqo) and succinyl-CoA : acetate CoA transferase (AarC), respectively (Mullins et al., 2008). Thus, it has been thought that these gene replacements play a key role in acetate oxidation, together with citrate synthase

(AarA), which makes the cells resistant to acetic acid. Therefore, we investigated the distribution of these four genes in five AAB genomes. We classified these genes in Acetobacteraceae genomes. Table 1 shows the distribution of Mqo and AarC, as well as Mdh and SCS, in five AAB science genomes. Only G. diazotrophicus and A. pasteurianus have AarC, which is consistent with the similar habitats of the two genera as described in the Introduction. In addition, Mqo of AAB was phylogenetically divided into two groups: one is Mqo (type GGr) of G. oxydans and G. bethesdensis and the other that (type GaA) of G. diazotrophicus and A. pasteurianus (data not shown). Thus, it is possible to speculate that the ability to overoxidize acetic acid to water and carbon dioxide was acquired by obtaining the aarC and mqo (type GaA) genes after divergence from Gluconobacter. In contrast, Gluconobacter lacks the TCA cycle. These results are also in good agreement with the concatenated multigene analysis, suggesting that the divergence of Gluconobacter from the ancestor of the three genera, Gluconobacter, Gluconacetobacter, and Acetobacter, occurred first.

Fosamprenavir/ritonavir (FPV/r) has not yet been evaluated One c

Fosamprenavir/ritonavir (FPV/r) has not yet been evaluated. One concern regarding PI/r monotherapy is that control of viral replication in reservoirs may be limited. LPV, DRV and FPV have been found to reach therapeutic concentrations in cerebrospinal fluid (CSF) [8–10], whereas atazanavir concentrations have been found to be variable [11]. Nevertheless, some patients under PI monotherapy have shown viral replication in CSF despite viral control in blood [2,5,12]. Consistent with these findings, neurological symptoms have been reported in patients on monotherapy

with LPV and DRV [2,5]; however, no neurological manifestations have been reported in other monotherapy trials [1,3,6,7]. Data regarding PI monotherapy in the genital tract compartment are scarce and controversial [12–15]. The objective of this study was BIBW2992 mouse to investigate viral response to FPV/r monotherapy in plasma and reservoirs in patients virologically suppressed with standard therapy. A prospective, multicentre, single-arm pilot study was conducted. The inclusion criteria were age >18 years, treatment with a PI/r

or nonnucleoside reverse transcriptase inhibitor (NNRTI) plus two nucleoside reverse transcriptase inhibitors (NRTIs) for ≥6 months, treatment with FPV/r plus two NRTIs for ≥1 month before study entry, no previous virological failure (VF) on a PI, defined as a detectable viral load (VL) while receiving a PI with the presence of resistance mutations or a change of therapy, VL <40 HIV-1 selleck inhibitor RNA copies/mL for ≥6 months, CD4 >100 cells/μL at inclusion, and the provision of written consent. The study was approved by ethics committees and the Spanish Drug Agency. At study entry, the two NRTIs were stopped and patients continued

with FPV/r (700/100 mg/12 h). The primary endpoint was defined as the percentage of patients with therapeutic Tryptophan synthase failure by a noncompletion-equals-failure (NC=F) intent-to-treat analysis (ITT); thus, patients with VF (three consecutive plasma VLs >40 copies/mL or two consecutive VLs >500 copies/mL separated by 2 weeks) and those who discontinued therapy for any reason were considered to have therapeutic failure. Genotype resistance tests were performed when VF occurred. If no PI mutations were detected, the same NRTIs were reintroduced; if PI mutations were selected, the PI/r was changed, based on genotype testing. The planned study sample size was 30 patients. If more than five patients experienced VF during the study, patient enrolment would terminate. Semen samples were collected by self-masturbation at weeks 0, 24 and 48, and lumbar puncture was performed at week 24. VL was determined in plasma, semen and CSF [by real-time polymerase chain reaction (PCR); limit of detection (LOD) <40 copies/mL]. Plasma amprenavir trough concentrations [high-performance liquid chromatography (HPLC)/ultraviolet (UV); LOD 0.

2, inset lane 5) These results suggest that the anti-Candida com

2, inset lane 5). These results suggest that the anti-Candida compounds belong to the iturin group characterized check details by the presence of tyrosine residue and a lipid-soluble β-amino fatty acid (Peypoux et al., 1981; Besson & Michel, 1986; Stein, 2005; Volpon et al., 2007). The molecular masses of the three lipopeptide compounds were determined by MALDI-TOF/MS. The spectrum mass of a1, a2 and a3 showed homologues (M+Na)+ major peaks at m/z 1053.5, 1067.5 and 1081.5, respectively, suggesting that these compounds are homologue molecules exhibiting different

lengths in their fatty acid chain (CH2=14 Da). Moreover, the molecular masses of these anti-Candida compounds are very close to C14, C15 and C16 homologues of bacillomycin D described in previous reports (Peypoux et al., 1984; Moyne et al., 2001; Koumoutsi et al., 2004; Oleinikova et al., 2005). These results confirmed the presence of the bamC gene involved in the synthesis of bacillomycin D in B. subtilis B38 strain. The MIC and MFC values of the purified compounds were evaluated

against host pathogenic Candida strains and were compared with those of amphotericin B (Table 3). The most potent compound a3 containing 16 carbons in its fatty acid moiety had MFC values superior to those of amphotericin B against most pathogenic C. albicans species. Furthermore, a3 showed a twofold lower MFC value (59.07 μM) than that of amphotericin B (135.26 μM) against the pathogenic-resistant C. albicans sp. 311 FN. The compound a2 containing 15 carbons in the fatty acid moiety exhibited a moderate anti-Candida Dabrafenib nmr activity and was two- to GPX6 eightfold less active than a3. Moreover, compound a1, having the shortest fatty acid chain (14 carbons), showed a weak anti-Candida effect and was 8–32-fold less active than a3. Differential sensitivity of C. albicans toward these compounds could be related to the length of the acyl chain. Our data

suggest a direct correlation between the length of the acyl chain of these compounds and their anti-Candida activities. Previous reports have underlined the importance of the length of the lipid moiety of bacillomycin D and bacillopeptin lipopeptides in the inhibitory effect against various fungal species (Kajimura et al., 1995; Moyne et al., 2001). Members of the iturin family generally exhibit strong antifungal activity against a wide variety of fungi, by interacting with the cytoplasmic membrane causing pore formation (Besson & Michel, 1984; Maget-Dana & Peypoux, 1994). It is tempting to speculate that differences in the activity of the anti-Candida compounds are related to the deepness of the generated membrane pores. In fact, antifungal compounds with a long acyl chain could be entirely incorporated into the yeast membrane compared to those having shorter acyl chains that presumably cannot span a membrane (Maget-Dana & Ptak, 1995).