[FTIR characterization of the secondary structure of a staphylokinase variant (K35R) encapsulated within PLGA microspheres].
The secondary structure of a staphylokinase variant (K35R, DGR) encapsulated in poly (lactic-co-glycolic acid) (PLGA) microspheres was quantitatively examined by Fourier transform infrared (FTIR) spectroscopy. Resolution enhancement technique and Fourier deconvolution were combined with band with curve-fitting procedures to quantitate the spectral information from the amide I bands. Nine component bands were found under the broad, nearly featureless amide I bands and assigned to alpha-helix, beta-sheet, turn and irregular (random) structures. The changes of bands at 1 651 and 1 623 cm(-1) after encapsulation were discussed.
He
Jin-Tian
JT
College of Life Science, Hebei Normal University, Shijiazhuang 050016, China.
Wang
Gai-Zhen
GZ
Song
Hou-Yan
HY
D019344:Lactic Acid / Q000737:chemistry; D008666:Metalloendopeptidases / Q000737:chemistry* / Q000235:genetics; D008863:Microspheres; D011100:Polyglycolic Acid / Q000737:chemistry; D000077182:Polylactic Acid-Polyglycolic Acid Copolymer; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
D000077182:Polylactic Acid-Polyglycolic Acid Copolymer; D011100:Polyglycolic Acid; D019344:Lactic Acid; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus