Preparation, characterization, in vitro release and degradation of cathelicidin-BF-30-PLGA microspheres.
basic_science · Level V
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- Record sourced from PubMed, PMID 24963652.
- Also identified by DOI 10.1371/journal.pone.0100809 and PMC identifier 4071013.
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Abstract
Cathelicidin-BF-30 (BF-30), a water-soluble peptide isolated from the snake venom of Bungarus fasciatus containing 30 amino acid residues, was incorporated in poly(D,L-lactide-co-glycolide) (PLGA) 75∶25 microspheres (MS) prepared by a water in oil in water W/O/W emulsification solvent extraction method. The aim of this work was to investigate the stability of BF-30 after encapsulation. D-trehalose was used as an excipient to stabilize the peptide. The MS obtained were mostly under 2 µm in size and the encapsulation efficiency was 88.50±1.29%. The secondary structure of the peptide released in vitro was determined to be nearly the same as the native peptide using Circular Dichroism (CD). The ability of BF-30 to inhibit the growth of Escherichia coli was also maintained. The cellular relative growth and hemolysis rates were 92.16±3.55% and 3.52±0.45% respectively.
Medical subject headings
- Antimicrobial Cationic Peptides
- Drug Delivery Systems
- Lactic Acid
- Microspheres
- Peptide Fragments
- Polyglycolic Acid