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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/9393

Title: Enhancement of thermal stability and inhibition of protein aggregation by osmolytic effect of hydroxyproline
Authors: KAR, K
KISHORE, N
Keywords: molten globule state
alpha-lactalbumin
compatible solutes
human lysozyme
triple-helix
hen lysozyme
stabilization
transition
collagen
fibrillogenesis
Issue Date: 2007
Publisher: JOHN WILEY & SONS INC
Citation: BIOPOLYMERS, 87(5-6), 339-351
Abstract: A combination of spectroscopic, calorimetric, and microscopic studies to understand the effect of hydroxyproline on the thermal stability, conformation, biological activity, and aggregation of proteins has been investigated. Significantly increased protein stability and suppression of aggregation is achieved in the presence of hydroxyproline. For example, exceptional increase in the thermal stability of lysozyme up to 26.4 degrees C and myoglobin up to 31.8 degrees C is obtained in the presence of hydroxyproline. The increased thermal stability of the proteins is observed to be accompanied with significant rise of the catalytic activity. Hydroxyproline is observed to prevent lysozyme fibril formation in vitro. Fluorescence and circular dichroism studies indicate induction of tertiary structures of the studied proteins in the presence of hydroxyproline. Preferential hydration of the native state is found to be crucial for the mechanism of protein stabilization by hydroxyproline. We compared the effect of hydroxyproline to that of proline and observed similar increase in the activity and suppression of protein aggregation. The results demonstrate the use of hydroxyproline as a protein stabilizer and in the prevention of protein aggregation and fibril formation. (C) 2007 .
URI: http://dx.doi.org/10.1002/bip.20834
http://dspace.library.iitb.ac.in/xmlui/handle/10054/9393
http://hdl.handle.net/10054/9393
ISSN: 0006-3525
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