Nanoscale changes in protein reveal bone health
December 26th, 2009 - 6:09 pm ICT by IANS ( Leave a comment )Washington, Dec 26 (IANS) Using an atomic force microscope that details images of nano-structures, researchers have discovered changes in the collagen component of bone that indicate its health - a step which could lead to new methods of diagnosing osteoporosis.
Collagen, the most common protein in the mammalian body, is present in bones, teeth, tendons, skin and arteries, making up to 35 percent of the body’s protein. Bone is a composite material made up of a flexible collagen matrix impregnated with and surrounded by a stiffer, stronger mineral component.
Though much is known about the importance of bone health to overall health, there’s a critical lack of knowledge about the sub-microscopic structure of bone and how collagen and mineral - and the interactions between them - contribute to properties of healthy and diseased bone.
“Our initial question was, could we discover more about the nanoscale structure of the collagen in bone, using the technique of atomic force microscopy,” said Mark Banaszak Holl, University of Michigan (U-M) professor in chemistry and macromolecular science and engineering, who led the study.
This microscope - a futuristic imaging tool - measures and manipulates matter at the atomic level, works something like a phonograph with a motion detector attached to its needle.
As the tip systematically moves across a bumpy tissue surface, the motion detector records its every movement. The result is a 3-D image of the surface’s contours.
Using such an instrument, the researchers were able to see and measure key features of collagen fibrils in mouse bone.
Each collagen fibril is made up of many individual collagen molecules packed together in a staggered array that resembles a railroad track.
“As opposed to a single value, our data indicate that normal bone contains a distribution of collagen fibril spacings,” a U-M release quoted Holl as saying.
“This ability to measure fibril spacing and to distinguish between normal and diseased bone… also has important implications to the future diagnosis of disease in bone and perhaps other collagenous tissues,” Holl added.
These findings were published online in Bone.
- Where bone strength comes from - Nov 02, 2010
- Synthetic protein to help regenerate new tissues - Sep 11, 2011
- New discovery offers hope to sufferers of osteoarthritis - Oct 24, 2010
- Indian-American explores how ageing impacts bones - Dec 03, 2009
- Scientists find endogenous proteins in a 70-mn-yr-old marine lizard - May 03, 2011
- New mechanism to pave way for methods to screen Alzheimer's drugs - Aug 21, 2010
- Mother Nature's new gift to prevent and treat bone diseases - Feb 03, 2011
- Super-strong artificial collagen may help treat arthritis - Jan 13, 2010
- How peptides control crystal growth with 'switches, throttles and brakes' - Nov 24, 2009
- Scientists shed light on how bone's material flaws lead to disease - Aug 05, 2009
- Wrinkles reducing creams are 'waste of money' - Jan 17, 2011
- New discovery may lead to drug treatment possibilities for Alzheimer's - Feb 11, 2011
- Scientists record first ever image of molecule's structure - Aug 29, 2009
- Synchrotron-based imaging technique for ultra-clear pictures of tissues - Mar 21, 2011
- High-strain tendons repair less frequently than low strain tendons - May 26, 2010
Tags: atomic force microscope, atomic force microscopy, atomic level, banaszak, bone health, collagen fibrils, collagen matrix, collagen molecules, composite material, critical lack, fibril, initial question, macromolecular science, mark banaszak holl, microscopic structure of bone, motion detector, nano structures, nanoscale structure, railroad track, tissue surface