In Situ Identification
of Secondary Structures in
Unpurified Bombyx mori Silk Fibrils
Using Polarized Two-Dimensional Infrared Spectroscopy
Posted on 2022-11-28 - 07:46
The mechanical properties
of biomaterials are dictated by the interactions
and conformations of their building blocks, typically proteins. Although
the macroscopic behavior of biomaterials is widely studied, our understanding
of the underlying molecular properties is generally limited. Among
the noninvasive and label-free methods to investigate molecular structures,
infrared spectroscopy is one of the most commonly used tools because
the absorption bands of amide groups strongly depend on protein secondary
structure. However, spectral congestion usually complicates the analysis
of the amide spectrum. Here, we apply polarized two-dimensional (2D)
infrared spectroscopy (IR) to directly identify the protein secondary
structures in native silk films cast from Bombyx mori silk feedstock. Without any additional peak fitting, we find that
the initial effect of hydration is an increase of the random coil
content at the expense of the helical content, while the β-sheet
content is unchanged and only increases at a later stage. This paper
demonstrates that 2D-IR can be a valuable tool for characterizing
biomaterials.
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Giubertoni, Giulia; Caporaletti, Federico; Roeters, Steven J.; Chatterley, Adam S.; Weidner, Tobias; Laity, Peter; et al. (2022). In Situ Identification
of Secondary Structures in
Unpurified Bombyx mori Silk Fibrils
Using Polarized Two-Dimensional Infrared Spectroscopy. ACS Publications. Collection. https://doi.org/10.1021/acs.biomac.2c01156
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AUTHORS (8)
GG
Giulia Giubertoni
FC
Federico Caporaletti
SR
Steven J. Roeters
AC
Adam S. Chatterley
TW
Tobias Weidner
PL
Peter Laity
CH
Chris Holland
SW
Sander Woutersen
KEYWORDS
commonly used toolsapply polarized twoadditional peak fittingprotein secondary structureinvestigate molecular structuresunderlying molecular propertiesrandom coil contentprotein secondary structuresdimensional infrared spectroscopysecondary structuresinfrared spectroscopymechanical propertiessheet contenthelical contentwidely studiedvaluable tooltypically proteinssitu identificationpaper demonstratesmacroscopic behaviorlater stageinitial effectgenerally limitedfree methodsdirectly identifybuilding blocksamide spectrumabsorption bands