PMID- 18293954 OWN - NLM STAT- MEDLINE DCOM- 20080701 LR - 20171116 IS - 1520-6106 (Print) IS - 1520-5207 (Linking) VI - 112 IP - 11 DP - 2008 Mar 20 TI - Energy transfer photophysics from serum albumins to sequestered 3-hydroxy-2-naphthoic acid, an excited state intramolecular proton-transfer probe. PG - 3451-61 LID - 10.1021/jp074598+ [doi] AB - The steady-state and time-resolved studies of the sensitized emission of the excited-state proton transfer (ESIPT) probe 3-hydroxy-2-naphthoic acid (3HNA) when bound to bovine serum albumin (BSA) and human serum albumin (HSA) indicate that the nonradiative dipole-dipole Forster type energy transfer from Trp singlet state of proteins to the ESIPT singlet state of 3HNA is greater in the case of HSA. This is supported by the distance and the orientation of the donor-acceptor pair obtained from the protein-ligand docking studies. The docking studies of the complex of BSA-3HNA also indicate that Trp 134 rather than Trp 213 is involved in the energy transfer process. The local environment of Trp 134 in BSA rather than that of Trp 213 is perturbed because of interaction with 3HNA as revealed by the optical resolution of Trp 134 phosphorescence in the complex at 77 K. Docking studies support the larger rotational correlation time, thetac (approximately 50 ns), observed for Trp residue/residues in the complexes of HSA and BSA compared with that in the free proteins. FAU - Sardar, Pinki Saha AU - Sardar PS AD - Department of Chemistry, Presidency College, Calcutta 700 073, India. FAU - Samanta, Subhodip AU - Samanta S FAU - Maity, Shyam Sundar AU - Maity SS FAU - Dasgupta, Swagata AU - Dasgupta S FAU - Ghosh, Sanjib AU - Ghosh S LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20080223 PL - United States TA - J Phys Chem B JT - The journal of physical chemistry. B JID - 101157530 RN - 0 (Naphthols) RN - 0 (Protons) RN - 0 (Serum Albumin) RN - 27432CM55Q (Serum Albumin, Bovine) RN - 8DUH1N11BX (Tryptophan) RN - C7S9D784HX (3-hydroxy-2-naphthoic acid) SB - IM MH - Binding Sites MH - Energy Transfer MH - Naphthols/*chemistry MH - *Photochemistry MH - Physical Phenomena MH - *Physics MH - *Protons MH - Serum Albumin/*chemistry MH - Serum Albumin, Bovine/chemistry MH - Spectrometry, Fluorescence MH - Tryptophan/chemistry EDAT- 2008/02/26 09:00 MHDA- 2008/07/02 09:00 CRDT- 2008/02/26 09:00 PHST- 2008/02/26 09:00 [pubmed] PHST- 2008/07/02 09:00 [medline] PHST- 2008/02/26 09:00 [entrez] AID - 10.1021/jp074598+ [doi] PST - ppublish SO - J Phys Chem B. 2008 Mar 20;112(11):3451-61. doi: 10.1021/jp074598+. Epub 2008 Feb 23.