Microscale spatial heterogeneity of protein structural transitions in fibrin matrices.

ABSTRACT: Following an injury, a blood clot must form at the wound site to stop bleeding before skin repair can occur. Blood clots must satisfy a unique set of material requirements; they need to be sufficiently strong to resist pressure from the arterial blood flow but must be highly flexible to support large strains associated with tissue movement around the wound. These combined properties are enabled by a fibrous matrix consisting of the protein fibrin. Fibrin hydrogels can support large macroscopic strains owing to the unfolding transition of α-helical fibril structures to β sheets at the molecular level, among other reasons. Imaging protein secondary structure on the submicrometer length scale, we reveal that another length scale is relevant for fibrin function. We observe that the protein pol

SUBMITTER: Fleissner F 

PROVIDER: S-EPMC5566164 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature