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2016 ; 11
(9
): e0161951
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Bowstring Stretching and Quantitative Imaging of Single Collagen Fibrils via
Atomic Force Microscopy
#MMPMID27598334
Quigley AS
; Veres SP
; Kreplak L
PLoS One
2016[]; 11
(9
): e0161951
PMID27598334
show ga
Collagen is the primary structural protein in animals. Serving as nanoscale
biological ropes, collagen fibrils are responsible for providing strength to a
variety of connective tissues such as tendon, skin, and bone. Understanding
structure-function relationships in collagenous tissues requires the ability to
conduct a variety of mechanical experiments on single collagen fibrils. Though
significant advances have been made, certain tests are not possible using the
techniques currently available. In this report we present a new atomic force
microscopy (AFM) based method for tensile manipulation and subsequent nanoscale
structural assessment of single collagen fibrils. While the method documented
here cannot currently capture force data during loading, it offers the great
advantage of allowing structural assessment after subrupture loading. To
demonstrate the utility of this technique, we describe the results of 23 tensile
experiments in which collagen fibrils were loaded to varying levels of strain and
subsequently imaged in both the hydrated and dehydrated states. We show that
following a dehydration-rehydration cycle (necessary for sample preparation),
fibrils experience an increase in height and decrease in radial modulus in
response to one loading-unloading cycle to strain <5%. This change is not altered
by a second cycle to strain >5%. In fibril segments that ruptured during their
second loading cycle, we show that the fibril structure is affected away from the
rupture site in the form of discrete permanent deformations. By comparing the
severity of select damage sites in both hydrated and dehydrated conditions, we
demonstrate that dehydration masks damage features, leading to an underestimate
of the degree of structural disruption. Overall, the method shows promise as a
powerful tool for the investigation of structure-function relationships in
nanoscale fibrous materials.