PMID- 20113169
OWN - NLM
STAT- MEDLINE
DCOM- 20100714
LR  - 20171116
IS  - 1464-5246 (Electronic)
IS  - 0265-2048 (Linking)
VI  - 27
IP  - 3
DP  - 2010 May
TI  - Entrapment enhancement of peptide drugs in niosomes.
PG  - 272-80
LID - 10.3109/02652040903131293 [doi]
AB  - The objective of this study was to enhance the entrapment of various charged 
      peptide drugs [(bacitracin (BCT), insulin and bovine serum albumin (BSA)] in 
      niosomes by modifying the vesicular charge compositions. Cationic, anionic and 
      neutral niosomes were prepared from sorbitan monostearate (Span 60) or 
      polyoxyethylene sorbitan monostearate (Tween 61), cholesterol (CHL), 
      dimethyldioctadecylammonium bromide (DDAB) and/or dicetyl phosphate (DP) in 
      distilled water, by freeze dried empty liposome (FDEL) method. Morphology and 
      vesicular sizes of the vesicles were investigated by optical microscope, TEM, 
      X-ray diffractometry and dynamic light scattering. The entrapment efficiency of 
      the peptides in niosomes was determined by gel electrophoresis and gel 
      documentation. After reconstitution of the empty niosomal powder in phosphate 
      buffer pH 7.0 containing the peptide drugs, they were oligolamellar membrane 
      structure, with the sizes of 40-60 nm, except the neutral niosomes entrapped with 
      insulin and cationic niosomes entrapped with BSA which showed the sizes of 
      0.1-1.3 microm and 100-150 nm, respectively. The zeta potential values of 
      neutral, cationic and anionic niosomes entrapped with BSA, insulin and BCT were 
      -22.3 +/- 1.52, -30.7 +/- 2.92 and +22.68+/- 1.31 mV, respectively. The 
      entrapment efficiency of BSA, BCT and insulin in neutral niosomes (Tween 61/CHL 
      at 1 : 1 molar ratio) was 72.94, 69.89 and 10.26%, in cationic niosomes (Tween 
      61/CHL/DDAB at 1 : 1 : 0.05 molar ratio) was 84.54, 32.85 and 87.15% and in 
      anionic niosomes (Tween 61/CHL/DP at 1 : 1 : 0.05 molar ratio) was 50.13, 90.88 
      and 44.31%, respectively. The highest entrapment efficiency of BSA, BCT and 
      insulin at 72.94, 90.88 and 87.15 was observed in neutral, anionic and cationic 
      niosomes, respectively. The results from this study has suggested the appropriate 
      niosomal formulation to entrap the peptides with different charges and polarity 
      for pharmaceutical application.
FAU - Manosroi, Aranya
AU  - Manosroi A
AD  - Natural Products Research and Development Center (NPRDC), Science and Technology 
      Research Institute (STRI), Chiang Mai University, Chiang Mai 50200, Thailand. 
      pmpti005@chiangmai.ac.th
FAU - Khanrin, Penpan
AU  - Khanrin P
FAU - Werner, Rolf G
AU  - Werner RG
FAU - Gotz, Friedrich
AU  - Gotz F
FAU - Manosroi, Worapaka
AU  - Manosroi W
FAU - Manosroi, Jiradej
AU  - Manosroi J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Microencapsul
JT  - Journal of microencapsulation
JID - 8500513
RN  - 0 (Anti-Bacterial Agents)
RN  - 0 (Insulin)
RN  - 0 (Liposomes)
RN  - 1405-87-4 (Bacitracin)
RN  - 27432CM55Q (Serum Albumin, Bovine)
SB  - IM
MH  - Animals
MH  - Anti-Bacterial Agents/*administration & dosage
MH  - Bacitracin/*administration & dosage
MH  - Cattle
MH  - Insulin/*administration & dosage
MH  - Liposomes/*chemistry/ultrastructure
MH  - Particle Size
MH  - Serum Albumin, Bovine/*administration & dosage
EDAT- 2010/02/02 06:00
MHDA- 2010/07/16 06:00
CRDT- 2010/02/02 06:00
PHST- 2010/02/02 06:00 [entrez]
PHST- 2010/02/02 06:00 [pubmed]
PHST- 2010/07/16 06:00 [medline]
AID - 10.3109/02652040903131293 [doi]
PST - ppublish
SO  - J Microencapsul. 2010 May;27(3):272-80. doi: 10.3109/02652040903131293.