Direct measurement of the rupture force of single pair of decorin interactions.
Decorin is one important member of the family of small leucine-rich proteoglycans, which are widely distributed in connective tissues in the body such as tendon and ligament. Decorin may be responsible for collagen fibril connection in those tissues. A recent hypothesis suggests that decorin may bind to collagen with its core protein while binding to another decorin through the interaction with their glycosaminoglycan (GAG) chains. However, there is no direct evidence supporting this hypothesis to date. In this study, the interaction of decorin GAG chains was directly determined for the first time. The rupture force of single bonds between decorins (GAG chains interaction) was determined directly as 16.5+/-5.1 pN using a laser tweezers/interferometer single molecular nanomechanical testing system. This information can improve our understanding of the mechanical properties of connective tissues at the molecular level.
Liu
Xuhui
X
Department of Orthopedic Surgery, Baylor College of Medicine, Houston, TX 77030, USA.
Yeh
Ming-Long
ML
Lewis
Jack L
JL
Luo
Zong-Ping
ZP
D000818:Animals; D002417:Cattle; D058575:Decorin; D016326:Extracellular Matrix Proteins; D007834:Lasers; D011485:Protein Binding; D011509:Proteoglycans / Q000737:chemistry / Q000378:metabolism*; D013718:Tensile Strength
D058575:Decorin; D016326:Extracellular Matrix Proteins; D011509:Proteoglycans