| Title: |
Binding of the environmental pollutant naphthol to bovine serum albumin |
| Authors: |
Wu, Tuoqi; Wu, Qin; Guan, Shanyue; Su, Hengxi; Cai, Zejian |
| Contributors: |
Wu, TQ (reprint author), Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China.; Peking Univ, Coll Life Sci, Beijing 100871, Peoples R China.; S China Univ Technol, Sch Chem & Energy Engn, Guangzhou 510641, Peoples R China.; Sun Yat Sen Univ, Instrumental Anal & Res Ctr, Guangzhou 510275, Peoples R China. |
| Source: |
PubMed ; SCI ; EI |
| Publisher Information: |
biomacromolecules |
| Publication Year: |
2007 |
| Collection: |
Peking University Institutional Repository (PKU IR) / 北京大学机构知识库 |
| Subject Terms: |
STATE PROTON-TRANSFER; CIRCULAR-DICHROISM SPECTROSCOPY; SECONDARY-STRUCTURE; PROTEIN; 1-NAPHTHOL; FLUORESCENCE; NAPHTHALENE; THERMODYNAMICS; CONFORMATION; TRANSITIONS |
| Description: |
The interactions between naphthol and bovine serum albumin (BSA) were investigated by spectroscopy. Our results prove the formation of complex between naphthol and BSA. Hydrophobic interaction dominates in the association reaction. The isomers stack with the aromatic residues in their binding sites with different geometries. Effects of BSA on the excited-state proton transfer and fluorescence spectra of the isomers indicate the different characters of their binding sites. 1-Naphthol inserts deeply into a hydrophobic cavity whereas 2-naphthol is in a basic environment on the surface of BSA. Naphthol statically quenches the fluorescence of BSA in a concentration-dependent manner positively deviating from the linear Stern-Volmer equation. Naphthol binds near Trp-134 in the subdomain IA of the native BSA and is accessible to Trp-212 when BSA is unfolded by naphthol. The folding pattern of the main chain is altered at high naphthol concentration as revealed by the change in the secondary structure. The binding of 1-naphthol is more cooperative than that of 2-naphthol. The extent of cooperativity was estimated by the Hill equation. ; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000247107900019&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology ; Chemistry, Organic ; Polymer Science ; SCI(E) ; EI ; PubMed ; 77 ; ARTICLE ; 6 ; 1899-1906 ; 8 |
| Document Type: |
journal/newspaper |
| Language: |
English |
| Relation: |
673926; http://hdl.handle.net/20.500.11897/162630; WOS:000247107900019 |
| DOI: |
10.1021/bm061189v |
| Availability: |
https://hdl.handle.net/20.500.11897/162630; https://doi.org/10.1021/bm061189v |
| Accession Number: |
edsbas.B655C302 |
| Database: |
BASE |