title: [FTIR characterization of the secondary structure of a staphylokinase variant (K35R) encapsulated within PLGA microspheres].
abstract: 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.
authors.affiliation: College of Life Science, Hebei Normal University, Shijiazhuang 050016, China.
authors.forename: Jin-Tian
authors.initials: JT
authors.lastname: He
authors.forename: Gai-Zhen
authors.initials: GZ
authors.lastname: Wang
authors.forename: Hou-Yan
authors.initials: HY
authors.lastname: Song
mesh_terms: 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*
chemical_list: D000077182:Polylactic Acid-Polyglycolic Acid Copolymer; D011100:Polyglycolic Acid; D019344:Lactic Acid; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus