Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin

Table 2

Secondary structure evaluation from far-UV cirular dichroism spectra.^(a)

Secondary Structure	HSA(b) (%)	HSA/CLP-A(b) (%)
Helix	46	41
Antiparallel	8	9
Parallel	6	6
Beta-Turn	15	16
Rndm. Coil	27	29
Total Sum	102	101

(a)CDNN V2.1 software was used to evaluate the secondary structure using the “complex” spectra category and the 210–260 nm region of the spectra.
(b)HSA (18 𝜇M), and HSA/CLA (18 𝜇M, 50 𝜇M) were in in 10 mM PBS, 5% DMSO, pH = 7.4 buffer.