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Probing hemoglobin confinement inside submicron silica tubes using synchrotron SAXS and electrochemical response.
MedLine Citation:
PMID:  23354357     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The configuration of hemoglobin in solution and confined inside silica nanotubes has been studied using synchrotron small angle X-ray scattering and electrochemical activity. Confinement inside submicron tubes of silica aid in preventing protein aggregation, which is vividly observed for unconfined protein in solution. The radius of gyration (R (g)) and size polydispersity (p) of confined hemoglobin was found to be lower than that in solution. This was also recently demonstrated in case of confined hemoglobin inside layered polymer capsules. The confined hemoglobin displayed a higher thermal stability with R (g) and p showing negligible changes in the temperature range 25-75 °C. The differences in configuration between the confined and unconfined protein were reflected in their electrochemical activity. Reversible electrochemical response (from cyclic voltammograms) obtained in case of the confined hemoglobin, in contrary to the observance of only a cathodic response for the unconfined protein, gave direct indication of the differences between the residences of the electroactive heme center in a different orientation compared to that in solution state. The confined Hb showed loss of reversibility only at higher temperatures. The electron transfer coefficient (α) and electron transfer rate constant (k (s)) were also different, providing additional evidence regarding structural differences between the unconfined and confined states of hemoglobin. Thus, absence of any adverse effects due to confinement of proteins inside the inorganic matrices such as silica nanotubes opens up new prospects for utilizing inorganic matrices as protein "encapsulators", as well as sensors at varying temperatures.
Authors:
Soumit S Mandal; Brindha Nagarajan; H Amenitsch; Aninda J Bhattacharyya
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-29
Journal Detail:
Title:  European biophysics journal : EBJ     Volume:  -     ISSN:  1432-1017     ISO Abbreviation:  Eur. Biophys. J.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8409413     Medline TA:  Eur Biophys J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore, 560012, India.
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