Amphiphilic poly(Ala)-b-poly(Sar) microspheres loaded with hydrophobic drug.
Amphiphilic block polypeptides, (Ala)m(Sar)n, were synthesized. Transmission electron microscopy showed that three kinds of block polypeptides, (Ala)42(Sar)21, (Ala)34(Sar)22, and (Ala)34(Sar)27, formed spherical aggregates in water. Dynamic light scattering measurement revealed that the average diameters of (Ala)42(Sar)21 and (Ala)34(Sar)22 aggregates were in the range of 80-90 nm, whilst that of (Ala)34(Sar)27 was about 30 nm. The polypeptides in aqueous solution took a beta-sheet structure, while they took an alpha-helical conformation in trifluoroethanol. These polypeptide aggregates took up 8-anilinonaphthalene-1-sulfonate (ANS), and the capacity of the aggregates for ANS decreased in the order of (Ala)42(Sar)21 > (Ala)34(Sar)22 > (Ala)34(Sar)27. Sumithion, which is a commercial agricultural insecticide, was also taken up by the polypeptide aggregates. When increasing amounts of Sumithion were introduced, (Ala)42(Sar)21 aggregates kept their shape, but (Ala)34(Sar)27 aggregate increased in size. These different behaviors of the polypeptide aggregates were discussed in terms of different structure of aggregates.
Department of Material Chemistry, Kyoto University, Japan.
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Kidchob
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Kimura
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Imanishi
D000409:Alanine / Q000737:chemistry*; D002942:Circular Dichroism; D016503:Drug Delivery Systems; D005278:Fenitrothion / Q000737:chemistry; D007306:Insecticides / Q000737:chemistry; D008823:Micelles; D010316:Particle Size; D010455:Peptides / Q000138:chemical synthesis*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012521:Sarcosine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D007306:Insecticides; D008823:Micelles; D010455:Peptides; D000409:Alanine; D005278:Fenitrothion; D012521:Sarcosine