Rapoport H Scott, Shadwick Robert E
Marine Biology Research Division, Scripps Institution of Oceanography, La Jolla, California 92093-0202, USA.
Biomacromolecules. 2002 Jan-Feb;3(1):42-50. doi: 10.1021/bm0155470.
Egg capsule material serves as a putative protection mechanism for developing snail embryos facing the perils of the marine environment. We conducted the first quantitative study of this acellular structural protein with the goals of characterizing its chemical and mechanical properties and the relationship of these properties to its biological protective function. We have found that this protein polymer exhibits long-range elasticity with an interesting recoverable yield evidenced by an order of magnitude decrease in elastic modulus (apparent failure) that begins at 3%-5% strain. This material differs significantly from other common structural proteins such as collagen and elastin in mechanical response to strain. Qualitative similarities in stress/strain behavior to keratin, another common structural protein, are more than coincidental when composition and detailed mechanical quantification are considered. This suggests the possibility of alpha-helical structure and matrix organization that might be similar in these two proteins. Indeed, the egg capsule protein may be closely related to vertebrate keratins such as intermediate filaments. We conclude that while this material's bimodal tensile properties may serve as useful protection against the impact loading egg capsules encounter in the intertidal zone, the full biological importance of these capsules is not known.
卵囊材料作为一种假定的保护机制,为发育中的蜗牛胚胎抵御海洋环境的危险。我们对这种无细胞结构蛋白进行了首次定量研究,旨在表征其化学和力学性质,以及这些性质与生物保护功能之间的关系。我们发现,这种蛋白质聚合物表现出长程弹性,具有有趣的可恢复屈服特性,弹性模量(表观失效)在3%-5%应变时开始下降一个数量级,即为证据。这种材料在对应变的力学响应方面与其他常见结构蛋白(如胶原蛋白和弹性蛋白)有显著差异。当考虑到组成和详细的力学量化时,其应力/应变行为与另一种常见结构蛋白角蛋白在定性上的相似性就不仅仅是巧合了。这表明这两种蛋白质可能具有相似的α-螺旋结构和基质组织。事实上,卵囊蛋白可能与脊椎动物角蛋白(如中间丝)密切相关。我们得出结论,虽然这种材料的双峰拉伸性能可能有助于保护卵囊免受潮间带所遇到的冲击载荷,但这些卵囊的全部生物学重要性尚不清楚。