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First published online February 20, 2004
Journal of Experimental Biology 207, 1127-1135 (2004)
Published by The Company of Biologists 2004
doi: 10.1242/jeb.00859

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The effect of molluscan glue proteins on gel mechanics

J. M. Pawlicki¹, L. B. Pease¹, C. M. Pierce¹, T. P. Startz¹, Y. Zhang² and A. M. Smith^1,*

¹ Department of Biology, Ithaca College, Ithaca, New York 14850, USA
² Department of Materials Science and Engineering, Cornell University, Ithaca, New York 14850, USA

View larger version (15K): [in a new window]   Fig. 1. Elution profile of L. irrorata adhesive mucus on a sephacryl S-400 column. The protein peak corresponds to a molecular mass of roughly 10–100 kDa and the carbohydrate peak corresponds to roughly 1000 kDa, based on calibration of the column with BSA (66 kDa), ferritin (440 kDa) and blue dextran (2000 kDa).

View larger version (91K): [in a new window]   Fig. 2. Examples of the qualitative effect of glue proteins from L. irrorata on gel mechanics. Samples were mixed in a microcentrifuge tube and poured or scooped out. Samples with glue proteins (0.5–1 mg ml–1) are on the right (Adhesive). Samples with the same concentration of BSA are on the left (Control). (A) 0.6% agar, (B) 2% polygalacturonic acid.

View larger version (86K): [in a new window]   Fig. 3. Identification of glue proteins from slug and land snail glue. (A) SDS-PAGE comparison between equal amounts of trail and adhesive mucus (glue) from the slug A. subfuscus. Arrowheads mark the 15 and 61 kDa proteins that are significantly more common in the adhesive mucus. (B) SDS-PAGE comparison between roughly equal amounts of trail and adhesive mucus from the land snail H. aspersa. Molecular mass markers are in the right lane, from top to bottom: 205, 116, 97, 84, 66, 55, 45 and 36 kDa.

View larger version (15K): [in a new window]   Fig. 4. The effect of different concentrations of H. aspersa glue proteins on citrus pectin mechanics. The storage modulus of 2% citrus pectin was measured with a dynamic rheometer. Gels contained different concentrations of glue proteins or BSA as a control. Three comparisons were performed at each concentration between 0.1 and 1 mg ml–1, and two comparisons were performed at each concentration above 1 mg ml–1 (except at 1.3 mg ml–1, which had only one trial). Values are means ± S.E.M. Note that the error bars do not show up on most of the controls because the variability is so small.

View larger version (13K): [in a new window]   Fig. 5. The effect of H. aspersa glue proteins on polymers with different degrees of charge. The storage moduli were measured with a dynamic rheometer. Gels contained 1 mg ml–1 glue proteins (dark bars) or 1 mg ml–1 BSA as a control (light bars). Agarose (0.2%, N=5), apple pectin (2%, N=7) and methylcellulose (2%, N=6) are neutral or less charged than agar (0.6%, N=7), citrus pectin (2%, N=7) and carboxymethylcellulose (2%, N=7). Values are means ± S.E.M. Asterisks indicate a significant difference (t-test or Wilcoxon two-sample test, P<0.05).

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