TY - JOUR

T1 - Sacrificial Bonds in Polymer Brushes from Rat Tail Tendon Functioning as Nanoscale Velcro

AU - Gutsmann, Thomas

AU - Hassenkam, Tue

AU - Cutroni, Jacqueline A.

AU - Hansma, Paul K.

N1 - Funding Information: This work was supported by the by the National Institutes of Health under Award No. GM65354, the National Science Foundation, through the MRL Program under Award No. DMR00-80034, the NASA/URETI Bioinspired Materials program under award NCC-1-02037, the USARL Institute for Collaborative Biotechnology (ICB) under award DAAD19-03-D-0004, Veeco, the Danish Research Council (STVF), and the Deutsche Forschungsgemeinschaft (project GU 568/2-1).

PY - 2005

Y1 - 2005

N2 - Polymers play an important role in many biological systems, so a fundamental understanding of their cross-links is crucial not only for the development of medicines but also for the development of biomimetic materials. The biomechanical movements of all mammals are aided by tendon fibrils. The self-organization and biomechanical functions of tendon fibrils are determined by the properties of the cross-links between their individual molecules and the interactions among the cross-links. The cross-links of collagen and proteoglycan molecules are particularly important in tendons and, perhaps, bone. To probe cross-links between tendon molecules, we used the cantilever tip of an atomic force microscope in a pulling setup. Applying higher forces to rat tail tendon molecules with the tip led to a local disruption of the highly organized shell of tendon fibrils and to the formation or an increase of a polymer brush of molecules sticking out of the surface. The cross-linking between these molecules was influenced by divalent Ca2+ ions. Furthermore, the molecules of the polymer brush seemed to bind back to the fibrils in several minutes. We propose that sacrificial bonds significantly influence the tendon fibrils' self-organization and self-healing and therefore contribute to toughness and strength.

AB - Polymers play an important role in many biological systems, so a fundamental understanding of their cross-links is crucial not only for the development of medicines but also for the development of biomimetic materials. The biomechanical movements of all mammals are aided by tendon fibrils. The self-organization and biomechanical functions of tendon fibrils are determined by the properties of the cross-links between their individual molecules and the interactions among the cross-links. The cross-links of collagen and proteoglycan molecules are particularly important in tendons and, perhaps, bone. To probe cross-links between tendon molecules, we used the cantilever tip of an atomic force microscope in a pulling setup. Applying higher forces to rat tail tendon molecules with the tip led to a local disruption of the highly organized shell of tendon fibrils and to the formation or an increase of a polymer brush of molecules sticking out of the surface. The cross-linking between these molecules was influenced by divalent Ca2+ ions. Furthermore, the molecules of the polymer brush seemed to bind back to the fibrils in several minutes. We propose that sacrificial bonds significantly influence the tendon fibrils' self-organization and self-healing and therefore contribute to toughness and strength.

U2 - 10.1529/biophysj.104.056747

DO - 10.1529/biophysj.104.056747

M3 - Journal article

C2 - 15879470

AN - SCOPUS:23244436582

VL - 89

SP - 536

EP - 542

JO - Biophysical Society. Annual Meeting. Abstracts

JF - Biophysical Society. Annual Meeting. Abstracts

SN - 0523-6800

IS - 1

ER -