Abstract:
:The common blue marine mussel adheres to underwater surfaces using an adhesive protein (Mefp-1) extruded from its foot. This highly hydroxylated protein contains a number of unusual amino acids, including 3,4-dihydroxyphenylalanine (DOPA), which is thought to contribute to the crosslinking of the extruded threads and adhesion to the substratum. Mefp-1 adheres to a wide variety of surfaces and is ultimately biodegradable. In this study we use surface-enhanced Raman spectroscopy (SERS) to characterize the adsorption of DOPA-containing peptides on colloidal gold. The peptides are simplified fragments of the Mefp-1 consensus decapeptide repeat, Ala-Lys-Pro-Ser-Tyr-DHP-Hyp-Thr-DOPA-Lys. Our results show that the peptides TDeltaKA, PTDeltaKA, and PPTDeltaKA (where Delta represents DOPA) coordinate to the gold surface through the catechol oxygens of the DOPA residue and through primary amine groups. The diproline sequence introduces conformational constraints that influence the conformations of the adsorbed peptides. These findings lay the groundwork for developing synthetic adhesives for underwater and medical applications.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Akemi Ooka A,Garrell RLdoi
10.1002/(SICI)1097-0282(2000)57:2<92::AID-BIP6>3.0subject
Has Abstractpub_date
2000-01-01 00:00:00pages
92-102issue
2eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(2000)57:2<92::AID-BIP6>3.0journal_volume
57pub_type
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