Deciphering the fluorescence resonance energy transfer signature of 3-pyrazolyl 2-pyrazoline in transport proteinous environment.
In the present investigation, an attempt has been made to study the interaction of newly synthesized bioactive compound 3-pyrazolyl 2-pyrazoline (PZ) with model transport proteins, bovine serum albumin (BSA), and human serum albumin (HSA) employing steady state and time-resolved fluorescence technique. We have focused on fluorescence resonance energy transfer (FRET) between excited tryptophan in transport proteins to transport-proteins-bound PZ. An efficient Forster-type resonance energy transfer from the tryptophan residues to PZ indicates that PZ binds in the vicinity of the tryptophan residue. Binding of protein to that bioactive compound without changing conformation of primary and secondary structure of protein has been monitored using circular dichroism (CD) study.
Banerjee
Paltu
P
Department of Chemistry, Jadavpur University, Kolkata 700032, India.
Pramanik
Smritimoy
S
Sarkar
Arindam
A
Bhattacharya
Subhash Chandra
SC
D000418:Albumins / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D031541:Fluorescence Resonance Energy Transfer; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011720:Pyrazoles / Q000737:chemistry*; D014364:Tryptophan / Q000737:chemistry
C544223:3-pyrazolyl 2-pyrazoline; D000418:Albumins; D011720:Pyrazoles; D014364:Tryptophan