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Synthesis and Characterization of Mussel Adhesive Peptides
Mussels, marine organisms, attach to underwater surfaces by making a byssus, which is an extra-corporeal bundle of tiny tendons attached distally to a foreign surface and proximally by insertion of the root into the byssal retractor muscles. The interaction exterior of byssus and marine surface is a...
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| Materialtyp: | Dissertation |
| Språk: | engelska |
| Publicerad: |
Philipps-Universität Marburg
2005
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| Länkar: | PDF-fulltext |
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| Sammanfattning: | Mussels, marine organisms, attach to underwater surfaces by making a byssus, which is an extra-corporeal bundle of tiny tendons attached distally to a foreign surface and proximally by insertion of the root into the byssal retractor muscles. The interaction exterior of byssus and marine surface is an adhesive plaque that contains different proportion of five mytilus edulis adhesive proteins (mefp-1 to 5). Relatively high contains of Lys, L-3,4-dihydroxyphenylalanine (DOPA), trans-4-hydroxyproline, and trans-2,3-cis-3,4-dihydroxyproline formulates MAPs as an adhesive protein. Derivation of synthetic bio-adhesives from MAPs have been limited due to fairly unsuccessful synthesize adhesive polypeptides and poor yield in extraction from biological source.
In this study, syntheses of mussel adhesive protein analogues have been performed. Several oligomers and polymers were synthesized with the comibation of bicyclic dipeptide building blocks, DOPA, Lys and Tyr. Use of bicyclic dipeptide building block has advantage over use of Hyp and Ser as former is expensive and latter needs side chain protection. Molecular structure, mass and size of these polymers were characterized using various techniques like NMR, MALDI, and GPC. The adhesive property of these polymers was tested using DOSY NMR experiment and AFM spectroscopy. Results obtained using AFM shows adhesion of poly-Lys-Bic-Tyr to graphite surface. These results open up a wide area in which finely tuned adhesive synthetic bio-polymers can be synthesized. |
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| DOI: | 10.17192/z2005.0111 |