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Synthesis and Surface Chemical Properties of Adhesive Protein of the Asian Freshwater Mussel, Limnoperna fortunei
Author(s) -
Ohkawa Kousaku,
Ichimiya Kengo,
Nishida Ayako,
Yamamoto Hiroyuki
Publication year - 2001
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/1616-5195(20011201)1:9<376::aid-mabi376>3.0.co;2-c
Subject(s) - biofouling , mussel , adhesive , wetting , freshwater bivalve , adsorption , chemistry , substrate (aquarium) , protein adsorption , contact angle , chemical engineering , biochemistry , organic chemistry , membrane , biology , bivalvia , layer (electronics) , ecology , mollusca , engineering
The adhesive polydecapeptide poly(Lys‐Pro‐Thr‐Gln‐Tyr‐Ser‐Asp‐Glu‐Tyr‐Lys) (average repeating number, n = 5), which is the consensus sequence of the Asian freshwater mussel Limnoperna fortunei adhesive protein (Lffp), has been synthesized by the polycondensation of the active esters. The surface chemical experiments revealed the following characteristics of the freshwater adhesive protein: (i) wettability of the Lffp solution is affected by the polar component value ( γ s p ) of the surface free energy of the substrate, and a substrate having a γ s p less than 10 mJ·m –2 exhibits a reduced wettability of the Lffp solution; (ii) the comparison of wettability of native Lffp with synthetic Lffp suggests that the decapeptide sequence, ‐Lys‐Pro‐Thr‐Gln‐Tyr‐Ser‐Asp‐Glu‐Tyr‐Lys‐, contributes to the interaction with the underwater surface; (iii) the Lffp tends to adsorb on nonpolar surfaces that have a low γ s p value; and (iv) the adsorption ability of the freshwater adhesive protein is less than that of the marine adhesive protein because of the higher hydrophilicity of the freshwater adhesive protein. An antifouling examination indicated that a γ s p value of the substrate surface of less than 10 mJ·m –2 should achieve a higher antifouling effect towards the L. fortunei attachment. These results are the first findings for the development of a freshwater antifouling strategy based on the molecular mechanism underlying the attachment of L. fortunei .