Abstract：
:End-functional 2-methacryloyloxyethyl phosphorylcholine (MPC) co-polymers containing two different monomer units, 2-hydroxyethyl methacrylate (HEMA) and n-butyl methacrylate (BMA), with varying hydrophilicities were synthesized to investigate the effect of the conjugated hydrophilic polymer on the heat-induced conformational changes of a protein. MPC co-polymer-conjugated proteins containing the HEMA unit (PMH) could withstand thermal conformational changes better than those containing the more hydrophobic BMA unit (PMB). The changes in protein tertiary structures were estimated via the excitation of tryptophan. PMH-conjugated proteins could withstand heat-induced intensity changes better than the PMB-conjugated proteins. Thus, hydrophilic units in the conjugated polymer are probably essential in suppressing the heat-induced conformational changes of a protein. The changes in secondary and tertiary structures of poly(MPC)-(PMPC) and poly(HEMA) (PHEMA)-conjugated proteins were compared to validate the effect of MPC units on heat-induced conformational change. Although the thermally induced conformational changes in the secondary and tertiary structures of PHEMA-conjugated proteins were partially suppressed, the effect on PMPC-conjugated proteins was much greater, with significant conformational preservation. This is due to the specific hydration state of the hydrophilic PMPC chain, which reduces interaction between the protein molecules.
journal_name
Acta Biomaterjournal_title
Acta biomaterialiaauthors
Seo JH,Matsuno R,Lee Y,Konno T,Takai M,Ishihara Kdoi
10.1016/j.actbio.2010.11.027subject
Has Abstractpub_date
2011-04-01 00:00:00pages
1477-84issue
4eissn
1742-7061issn
1878-7568pii
S1742-7061(10)00534-9journal_volume
7pub_type
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