羥脯胺酸醣化修飾對膠原蛋白穩定性與自組裝之影響

黃佩雯

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羥脯胺酸醣化修飾對膠原蛋白穩定性與自組裝之影響

The effects of glycosylated (2S,4R)-hydroxyproline on collagen stability and self-assembly

黃佩雯 , Masters　　Advisor：洪嘉呈　　

繁體中文

膠原蛋白；半乳糖； collagen ； galactose

Abstract │ Reference (35) │ Altmetrics

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Collagen, the most abundant protein in mammalian tissues, has been widely used in biomedical materials. Many researchers have been performing various modifications on collagen to increase its applicability. Different non-covalent interactions were also applied to promote the self-assembly of collagen into higher order structure. Collagen is a right-handed triple helix, and each helix is a left-handed polyproline type II structure containing many (X-Y-Gly)n repeats. On the other hand, carbohydrates are a necessity to organism and play an important role in biological functions. 
    In this work, we modified (2S,4R)-hydroxyproline with 1.2,3,4,6-penta-O-acetyl-β-D-galactopyranoside and synthesized a series of collagen-related peptides containing this modified amino acid to study the consequences of glycosylation on collagen stability and self-assembly.  
    CD measurements indicate that glycosylation will destabilize the collagen triple helices. However, TEM shows that the modification promotes the self-assembly of collagen-related peptides into higher-order structures, suggesting that glycosylation could enhance the interactions between collagen-related peptides to speed their assembly.

Reference ( 35 ) 〈TOP〉

1. Bella, J., Brodsky, B., and Berman, H. M. (1995) Hydration structure of a collagen peptide, Structure 3, 893-906.
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3. Griffon, N. B., V.; Dieryck, W.; Domoulin, A.; Paginer, J.; Poyart, C.;Marden, M. C. (1998) tetramer-dimer equilibrium of oxyhemoglobin mutants determined from auto-oxidation rates, Protein Sci. 7, 673-680.
連結：
4. Prockop, D. J. K., K. I. (1995) Collagens: molecular biology, diseases, and potentials for therapy, Annu. Rev. Biochem. 64, 403-434.
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5. Prockop, D. J. (1998) What holds us together? Why do some of us fall apart? What can we do about it?, Matrix Biol. 16, 519-528.
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6. prockop, D. J. (1999) Hopkins Memorial Medal lecture. Pleasant surprises en route from the biochemistry of collagen to attempts at gene therapy, Biochem. Soc. Trans, 15-31.
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