TY  - JOUR
ID  - open275
UR  - http://www.sciencedirect.com/science/article/pii/S0006291X02965496
IS  - 4
A1  - Kundu, Bishwajit
A1  - Shukla, Anshuman
A1  - Guptasarma, Purnananda
N2  - A phage-displayed library of peptides (12-mer) was screened for the ability to bind to thermally aggregated bovine carbonic anhydrase (BCA), with a view toward examining whether peptides possessing this ability might bind to partially structured intermediates on the protein's unfolding pathway and, therefore, constitute useful tools for manipulation of the kinetic partitioning of molecules between the unfolded and aggregated states. Two peptides [N-HPSTMGLRTMHP-C and N-TPSAWKTALVKA-C] were identified and tested. While neither showed thermal aggregation autonomously, both peptides individually elicited remarkable increases in the levels of thermal aggregation of BCA. A possible explanation is that both peptides bind to surfaces on molten BCA that are not directly involved in aggregation. Such binding could slow down interconversions between folded and unfolded states and stabilize aggregation-prone intermediate(s) to make them more prone to aggregation, while failing to achieve any steric prevention of aggregation. The approach has the potential of yielding useful aggregation-aiding/inhibiting agents, and may provide clues to whether amorphous aggregates are "immobilized" forms of folding intermediates.
VL  - 291
TI  - Manipulation of unfolding-induced protein aggregation by peptides selected for aggregate-binding ability through phage display library screening.
AV  - restricted
EP  - 7
N1  - Copyright of this article belongs to Elsevier Science.
Y1  - 2002/03/08/
PB  - Elsevier Science
JF  - Biochemical and biophysical research communications
KW  - thermal unfolding; protein aggregation; phage display; folding intermediates
SN  - 0006-291X
SP  - 903
ER  -