Characterization of a Dimeric Unfolding Intermediate of Bovine Serum Albumin Under Mildly Acidic Condition.
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
Characterization of a Dimeric Unfolding Intermediate of Bovine Serum Albumin Under Mildly Acidic Condition.
|
|
| Creator |
Brahma, Amrita
Mandal, Chhabinath Bhattacharyya, Debasish |
|
| Subject |
Structural Biology & Bioinformatics
|
|
| Description |
Protein aggregation is a well-known phenomenon related to serious medical implications. Bovine serum albumin (BSA), a structural analogue of human serum albumin, has a natural tendency for aggregation under stress conditions. While following effect of moderately acidic pH on BSA, a state was identified at pH 4.2 having increased light scattering capability at 350 nm. It was essentially a dimer devoid of
disulphide linked large aggregates as observed from Fspin column_ experiments, gel electrophoresis and ultra-centrifugations. Its surface hydrophobic character was comparable to the native conformer at pH 7.0 as observed by the extraneous fluorescence probes pyrene and pyrene maleimide but its interactions with 1-anilino 8-naphthelene sulphonic acid was more favorable. Dimerization was irreversible between pH 4.2 and 7.0 even after treatment with DTT. The role of the only cysteine-34 residue was investigated where modification with reagents of
arm length bigger than 6 A° prevented dimerization. Molecular modeling of BSA indicated that cys-34 resides in a cleft of 6 A° depth. This indicated that the area surrounding the cleft plays important role in inducing the dimerization.
|
|
| Date |
2005
|
|
| Type |
Article
PeerReviewed |
|
| Format |
application/pdf
|
|
| Identifier |
http://www.eprints.iicb.res.in/1085/1/BIOCHIMICA_ET_BIOPHYSICA_ACTA%2DPROTEINS_AND_PROTEOMICS%2C1751%2C_2_%2C_159%2D169_[38].pdf
Brahma, Amrita and Mandal, Chhabinath and Bhattacharyya, Debasish (2005) Characterization of a Dimeric Unfolding Intermediate of Bovine Serum Albumin Under Mildly Acidic Condition. Biochimica et Biophysica Acta, 1751 (2). pp. 159-169. |
|
| Relation |
http://dx.doi.org/10.1016/j.bbapap.2005.06.007
http://www.eprints.iicb.res.in/1085/ |
|