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Int. J. Mol. Sci. 2017, 18(3), 520; doi:10.3390/ijms18030520

Ovalbumin with Glycated Carboxyl Groups Shows Membrane-Damaging Activity

1
Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan
2
Department of Fragrance and Cosmetic Science, Kaohsiung Medical University, Kaohsiung 807, Taiwan
3
Department of Biotechnology, Kaohsiung Medical University, Kaohsiung 807, Taiwan
*
Author to whom correspondence should be addressed.
Academic Editor: Masatoshi Maki
Received: 12 January 2017 / Revised: 17 February 2017 / Accepted: 22 February 2017 / Published: 28 February 2017
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [3361 KB, uploaded 28 February 2017]   |  

Abstract

The aim of the present study was to investigate whether glycated ovalbumin (OVA) showed novel activity at the lipid-water interface. Mannosylated OVA (Man-OVA) was prepared by modification of the carboxyl groups with p-aminophenyl α-dextro (d)-mannopyranoside. An increase in the number of modified carboxyl groups increased the membrane-damaging activity of Man-OVA on cell membrane-mimicking vesicles, whereas OVA did not induce membrane permeability in the tested phospholipid vesicles. The glycation of carboxyl groups caused a notable change in the gross conformation of OVA. Moreover, owing to their spatial positions, the Trp residues in Man-OVA were more exposed, unlike those in OVA. Fluorescence quenching studies suggested that the Trp residues in Man-OVA were located on the interface binds with the lipid vesicles, and their microenvironment was abundant in positively charged residues. Although OVA and Man-OVA showed a similar binding affinity for lipid vesicles, the lipid-interacting feature of Man-OVA was distinct from that of OVA. Chemical modification studies revealed that Lys and Arg residues, but not Trp residues, played a crucial role in the membrane-damaging activity of Man-OVA. Taken together, our data suggest that glycation of carboxyl groups causes changes in the structural properties and membrane-interacting features of OVA, generating OVA with membrane-perturbing activities at the lipid-water interface. View Full-Text
Keywords: ovalbumin; glycation; carboxyl group; membrane-damaging activity ovalbumin; glycation; carboxyl group; membrane-damaging activity
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MDPI and ACS Style

Tang, C.-C.; Shi, Y.-J.; Chen, Y.-J.; Chang, L.-S. Ovalbumin with Glycated Carboxyl Groups Shows Membrane-Damaging Activity. Int. J. Mol. Sci. 2017, 18, 520.

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