In Vitro Activity of the Histatin Derivative P-113 against Multidrug-Resistant Pathogens Responsible for Pneumonia in Immunocompromised Patients
Open Access
- 1 March 2005
- journal article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 49 (3), 1249-1252
- https://doi.org/10.1128/aac.49.3.1249-1252.2005
Abstract
The in vitro activity of the histatin derivative P-113, alone or combined with eight antibiotics, was investigated against multidrug-resistant strains isolated from clinical specimens of immunocompromised patients with pneumonia. The gram-negative isolates were susceptible to P-113. S. aureus showed less susceptibility. Synergy was demonstrated when P-113 was combined with beta-lactams against gram-negative organisms.Keywords
This publication has 19 references indexed in Scilit:
- Potential Therapeutic Role of Histatin Derivative P‐113din Experimental Rat Models ofPseudomonas aeruginosaSepsisThe Journal of Infectious Diseases, 2004
- Bactericidal cationic peptides can also function as bacteriolysis-inducing agents mimicking beta-lactam antibiotics?; it is enigmatic why this concept is consistently disregardedMedical Hypotheses, 2004
- Lung Infections Associated with Cystic FibrosisClinical Microbiology Reviews, 2002
- P-113 d , an Antimicrobial Peptide Active against Pseudomonas aeruginosa , Retains Activity in the Presence of Sputum from Cystic Fibrosis PatientsAntimicrobial Agents and Chemotherapy, 2001
- Anticandida Activity Is Retained in P-113, a 12-Amino-Acid Fragment of Histatin 5Antimicrobial Agents and Chemotherapy, 2001
- The Lung in the Immunocompromised PatientRespiration, 1999
- Anti-lipopolysaccharide activity of histatins, peptides from human salivaCellular and Molecular Life Sciences, 1993
- Emergence of antibiotic resistance amongst Pseudomonas aeruginosa isolates from patients with cystic fibrosisJournal of Antimicrobial Chemotherapy, 1993
- Solid phase peptide synthesis utilizing 9‐fluorenylmethoxycarbonyl amino acidsInternational Journal of Peptide and Protein Research, 1990
- A family of wound healersNature, 1987