Use of a spectrofluorimetric method to monitor changes of human serum albumin thermal stability in the presence of polyamidoamine dendrimers.
Polyamidoamine (PAMAM) dendrimers' impact on human serum albumin thermal stability was investigated. Thermal denaturation profiles were determined from changes in the intrinsic fluorescence intensity. In the presence of dendrimers the shift of a denaturation temperature toward higher values was observed. It indicates a slight increase of protein stability upon dendrimers treatment.
Jokiel
M
M
Department of General Biophysics, University of Lodz, 12/16 Banacha St., 90-237, Lodz, Poland.
Klajnert
B
B
Bryszewska
M
M
D050091:Dendrimers; D006358:Hot Temperature; D006801:Humans; D011073:Polyamines / Q000737:chemistry*; D011489:Protein Denaturation; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013696:Temperature
D050091:Dendrimers; C104700:PAMAM Starburst; D011073:Polyamines; D012709:Serum Albumin