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pubmed-article:19743815pubmed:abstractTextWhile evidence is mounting that cells exploit protein unfolding for mechanochemical signal conversion (mechanotransduction), what mechanisms are in place to deal with the unwanted consequences of exposing hydrophobic residues upon force-induced protein unfolding? Here, we show that mechanical chaperones exist that can transiently bind to hydrophobic residues that are freshly exposed by mechanical force. The stretch-upregulated binding of albumin or casein to fibronectin fibers is reversible and does not inhibit fiber contraction once the tension is released.lld:pubmed
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pubmed-article:19743815pubmed:dateRevised2010-9-28lld:pubmed
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pubmed-article:19743815pubmed:articleTitleStretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein.lld:pubmed
pubmed-article:19743815pubmed:affiliationDepartment of Materials, ETH Zurich, CH-8093 Zurich, Switzerland.lld:pubmed
pubmed-article:19743815pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19743815pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:19743815pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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