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.
Highlights
BF-30 is a 30-residue peptide isolated from the venom of the snake Bungarus fasciatus, which exhibits broad antimicrobial activity against bacteria and fungi
Morphology characterization Microspheres prepared by the W/O/W emulsion/solvent evaporation/extraction method with a high yield of 76.6468.07% according to the equation (3)
To test the biological effect of the released peptide, we investigated the activity of release medium on the 1st, 10th, 11th,and 12th days against Escherichia coli, which is sensitive to BF30 [1,2]
Summary
BF-30 is a 30-residue peptide isolated from the venom of the snake Bungarus fasciatus, which exhibits broad antimicrobial activity against bacteria and fungi. The peptide has a short half-life in serum [3], which may be caused by proteases present in serum [4]. Attempts have been made to increase the stability of BF-30 by chemical modification of the peptide through pegylation to extend the half-life [5,6]. Pegylation is a chemical modification method for increasing the stability of peptide by conjugating PEG to peptide or protein, the process may have an effect on the therapeutic effect of the peptide [3]. An alternative route to improve stability is to formulate the chemically intact peptide in a suitable carrier vehicle [3]
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