surfaces of other cells, as well as adhere to a substrate called the extracellular matrix (ECM). These interactions with surfaces play a key role in stem cell growth and differentiation. And that got Kiessling thinking.
"If we want to control stem cell fates," she says, "maybe we could start to create surfaces of defined molecules, put stem cells down on them, and ask, 'What happens?'"
To this end, the researchers tethered 18 distinct protein fragments, known as peptides, to the surfaces of specially treated microscope slides. The peptides were arranged in a regular pattern of squares, each measuring one-half to three-quarters of a millimeter on a side.
Patterns of DNA and proteins on surfaces, known as arrays, are common tools in biological research. What sets Kiessling's arrays apart is the size and function of the square-shaped patches of peptides: They're roomy enough to let stem cells grow in them for up to a week, yet tiny enough to allow screening of hundreds of different conditions within a single square inch.
The peptides her team chose to test first come from a major protein component of the ECM called laminin. Laminin also makes up about 60 percent of Matrigel, an extract from mouse cells that often serves as a substrate for growing stem cells in culture.
In a series of weeklong experiments, the team placed human embryonic stem (ES) cells onto the squares in the arrays, set the arrays in a culture plate and added a culture medium on top. What they found is that five of the 18 surfaces - each displaying just a single peptide from laminin - did as well as the mixture Matrigel at growing human ES cells in their "blank slate," undifferentiated condition.
The researchers don't yet know why these particular laminin peptides promote human ES cell growth. But with them in hand, scientists can now take the next step of identifying the receptors or other molecules that the pept
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