Ignite Creation Date:
2025-12-26 @ 10:58 AM
Ignite Modification Date:
2026-01-13 @ 11:44 AM
Study NCT ID:
NCT06899906
Status:
RECRUITING
Last Update Posted:
2025-03-28
First Post:
2025-03-21
Is NOT Gene Therapy:
True
Has Adverse Events:
False
Brief Title:
Efficacy and Safety of Dalbavancin As Suppressive Therapy
Sponsor:
Hospices Civils de Lyon
Organization:
Study Overview
Official Title:
Efficacy and Safety of Dalbavancin As Suppressive Therapy
Status:
RECRUITING
Status Verified Date:
2025-03
Last Known Status:
None
Delayed Posting:
No
If Stopped, Why?:
Not Stopped
Has Expanded Access:
False
If Expanded Access, NCT#:
N/A
Has Expanded Access, NCT# Status:
N/A
Acronym:
DALBA-SAT
Brief Summary:
Dalbavancin (DAL) is a semi-synthetic antibiotic that belongs to the lipoglycopeptide family and is structurally derived from teicoplanin, respect of which it has two structural differences that enhance its anti-staphylococcal binding affinity and extend its half-life to between 149 and 250 hours. It achieves adequate tissue penetration in the skin, bones, joints, lung tissues, and peritoneal space, maintaining concentrations above the MIC for susceptible Gram-positive pathogen.
DAL is a bactericidal antimicrobial agent that binds the C-terminal D-alanyl-D-alanine on the bacterial cell wall, blocking trans-glycosylation and transpeptidation processes essential for cell wall synthesis. It seems also to be able to enhance neutrophil antibacterial activity improving PMNs' intracellular killing of MRSA. It has also a good antibiofilm activity, alone or in combination with other molecules. Like other glycopeptide molecules, DAL shares a similar spectrum of activity, with demonstrated in vitro activity against various Gram-positive bacteria, including Staphylococcus spp, Streptococcus spp and Enterococcus (faecium, and faecalis). Resistance to DAL is possible in these gram-positives bacteria, given to presence of enzymes that produce low-affinity binding precursors for the antibiotic's binding site. DAL is capable to overcome Van-B mechanism of resistance, but it results not active in producing Van-A strains.
The study objectives was to evaluate efficacy and safety of DAL treatment.
DAL is a bactericidal antimicrobial agent that binds the C-terminal D-alanyl-D-alanine on the bacterial cell wall, blocking trans-glycosylation and transpeptidation processes essential for cell wall synthesis. It seems also to be able to enhance neutrophil antibacterial activity improving PMNs' intracellular killing of MRSA. It has also a good antibiofilm activity, alone or in combination with other molecules. Like other glycopeptide molecules, DAL shares a similar spectrum of activity, with demonstrated in vitro activity against various Gram-positive bacteria, including Staphylococcus spp, Streptococcus spp and Enterococcus (faecium, and faecalis). Resistance to DAL is possible in these gram-positives bacteria, given to presence of enzymes that produce low-affinity binding precursors for the antibiotic's binding site. DAL is capable to overcome Van-B mechanism of resistance, but it results not active in producing Van-A strains.
The study objectives was to evaluate efficacy and safety of DAL treatment.
Detailed Description:
None
Study Oversight
Has Oversight DMC:
False
Is a FDA Regulated Drug?:
None
Is a FDA Regulated Device?:
None
Is an Unapproved Device?:
None
Is a PPSD?:
None
Is a US Export?:
False
Is an FDA AA801 Violation?: